Biology/BioChem Review Flashcards
(337 cards)
1
Q
Can a virus ever undergo meiosis?
A
No, they lack the “complex cellular machinery”.
2
Q
Natural killer cells are part of which immune system?
A
Innate
3
Q
NK and Cytolytic T cells do what?
A
Destruction of one’s own cells that are either cancerous or virus infected
4
Q
Innate immune system
A
cells and proteins that are always present and ready to mobilize and fight microbes at the site of infection.
1) physical epithelial barriers, 2) phagocytic leukocytes, 3) dendritic cells, 4) a special type of lymphocyte called a natural killer (NK) cell, and 5) circulating plasma proteins. 0-12 hr timeline
5
Q
Adaptive immune system
A
called into action against pathogens that are able to evade or overcome innate immune defenses.
humoral immunity, mediated by antibodies produced by B lymphocytes
cell-mediated immunity, mediated by T lymphocytes.
6
Q
Leukocytes are:
A
White blood cells. Types of leukocytes are: lymphocytes, neutrophils, basophils, eosinophils, monocytes, and macrophages
7
Q
Start codon:
A
AUG
8
Q
3 stop codons:
A
UAG, UAA, and UGA.
9
Q
Primary immune response:
A
occurs when an antigen comes in contact to the immune system for the first time. During this time the immune system has to learn to recognize antigen and how to make antibody against it and eventually produce memory lymphocytes. (B cells)
10
Q
Secondary Immune response:
A
occurs when the second time (3rd, 4th, etc.) the person is exposed to the same antigen. At this point immunological memory has been established and the immune system can start making antibodies immediately.
11
Q
Smooth ER:
A
Lipid synthesis/modification (but NOT lipid metabolism; many students get this confused. Lipids are made at the ER, but metabolized in the mitochondria).
12
Q
Tubulin:
A
a globular protein that polymerizes to form microtubules.
13
Q
Cytoskeleton:
A
scaffolding-like network of microfilaments, microtubules, and intermediate filaments that provides structure to the cell and creates a highway of sorts for intracellular transport.
14
Q
Actin:
A
a protein monomer that polymerizes to form microfilaments. Also forms thin filament portion of sarcomere.
15
Q
Microtubules:
A
Make up cilia and flagella. (9+2 arrangement)
16
Q
Adherens Junctions:
A
are found in epithelium and between cardiac muscle cells.
17
Q
Desmosomes:
A
occur in tissues subject to shear stress such as the epidermis.
18
Q
Endocrine signaling:
A
Hormones are manufactured and secreted by cells in the endocrine glands, travel in the bloodstream, then bind to receptors either on the cell surface (in the case of water-soluble hormones) or inside the cell (in the case of lipid-soluble hormones).
19
Q
Intracellular receptor:
A
Lipid-soluble hormones (e.g., steroids) do not require a plasma membrane surface receptor. They dissolve through the membrane and bind targets in the cytosol which often move to nucleus to act.
20
Q
Paracrine signaling: (Pair…acrine)
A
Signal molecules secreted by one cell bind to receptors on other cells in the local area. Neurotransmitters acting in the synaptic gap are an example of a paracrine response.
21
Q
Autocrine signaling: (auto: self)
A
Signal molecules secreted by a cell bind to receptors on that same cell.
22
Q
Intracrine signaling: (intra: within)
A
Signal molecules (usually steroids) bind to receptors inside the same cell that producedthem, without ever being secreted outside of the cell.
23
Q
Juxtacrine signaling:
A
Signaling requires direct contact between two cells.
24
Q
Histones:
A
the proteins around which the DNA helix is wrapped during the first step of DNA condensation to form a chromosome
25
Nucleosome:
a set of eight histone proteins in a cube
| shape with DNA coiled around it much like thread wound around a spool.
26
Centromere:
the region of the chromosome that joins the two sister chromatids
27
Kinetochore:
a specialized group of proteins to which the
| spindle fibers attach directly during mitosis/meiosis.
28
IPMATC:
```
Interphase: uncoiled chromosomes
Prophase: Cell membrane disolved
Metaphase: Chromosomes line up
Anaphase: Chromosomes are separated and begin migration
Telophase: Nuclear membranes reforming.
```
29
Mitosis:
Two (2) genetically identical, diploid daughter cells
30
Meiosis:
Four (4) genetically distinct, haploid daughter cells
31
When does crossing over occur?
During Prophase of Meiosis I
32
What makes up a nucleotide? 3 components
Base, Sugar, triphosphate
33
What are purines and what are pyrimidines?
Adenine and Guanine are Purines.
| Thymine and Cytosine are Pyrimidines, also Uracil is a pyrimidine.
34
Origin of replication:
the location on the chromosome where replication begins. For human chromosomes there are multiple origins.
35
Restriction endonucleases:
enzymes that cut DNA at specific pre-determined sequences.
36
Sticky ends:
are so named because the endonuclease cuts the DNA in a staggered fashion that leaves one side of the helix longer than the other
37
Recognition Sequence:
The specific base sequence recognized by the endonuclease
38
Vector:
a segment of DNA used to transfer a desired sequence into another cell.
39
Phage:
an abbreviated name for a bacteriophage (a virus that infects bacteria)
40
Gel electrophoresis:
mixture of molecules (usually nucleotide segments or proteins) is loaded onto a plate covered
with an agarose gel. A charged field is created across the gel. Because nucleotides are negatively
charged (due to the phosphate groups) they will be pulled through the gel toward the positive
side of the field, which is called the anode
41
Southern blot: PCR
Used to verify the presence/absence of a specific DNA sequence. It will also indicate the relative size of restriction fragments.
42
Northern BLot:
Nearly identical to a Southern Blot; used on RNA instead of DNA.
43
Western blot:
Same basic procedure and concepts as Northern and Southern blots; used on proteins segments instead of nucleotide segments. The probes used are radio-labeled antibodies rather than nucleotide sequences.
44
Eastern blot:
Similar to a Western blot, but used to verify post-translational modification. The probes used bind to lipids, carbohydrates and phosphates (i.e., the most common posttranslational modifications).
45
Ribosomal rRNA
is the polymer of which ribosomes are constructed. Remind students that ribosomes are assembled in the nucleolus. Ribosomes are a non-protein entity that act as enzymes in the polymerization of proteins, and are an example of a non-protein enzyme.
46
Transfer tRNA
the molecule that bridges the gap between mature mRNA and the assembled protein
47
Messenger mRNA
the complementary RNA strand copied from the DNA template strand. Has pre-mRNA which still contains non coding segments, and once removed has mature mRNA
48
Alternative Splicing:
refers to the fact that after introns are removed from the mRNA transcript, the exons can be assembled in any of a number of different orders—each variation resulting in a different protein.
49
Lactase:
the enzyme that digests lactose in bacteria.
50
post translational modification:
Occurs at the endoplasmic reticulum and the Golgi apparatus; usually includes addition of polysaccharides, lipids, or phosphates.
51
Nonsense mutation:
a mutation that changes a normal codon into a premature stop codon.
52
Frameshift mutation:
any mutation that changes the reading frame. This would be any insertion or deletion that does not occur in multiples of three.
53
Heritability in germ and somatic cells:
the next generation will ONLY receive the genetic information found in the sperm or egg cell they receive from each respective parent. Mutations to any or all somatic cells will not be incorporated into the offspring.
54
Incomplete penetrance:
when various individuals all have identical genotypes and yet some have the disease phenotype and others do not
55
Polygenic:
when many genes contribute to one phenotypic trait.
56
Pleiotropy:
describes the situation in which one single gene contributes to multiple phenotypic traits.
57
Mosaicism:
different cells within the same individual contain non-identical genotypes
58
Epigenetic:
refers to any heritable phenotype resulting from any process other than a change in the DNA sequence itself. epi like outside
59
What could be the cause of an unexpected ratio of genetic inheritance?
Linkage
60
Polymorphism:
random variations in genetic sequence among individuals. If beneficial, would stay in next generations.
61
Adaptive radiation:
the rapid formation of a variety of species from one ancestral species—usually characterized by a strong environment-species connection
62
In order for natural selection to occur: 2 things
Fitness advantage from polymorphism, this results in more offspring produced from this individual
63
Convergent evolution:
results when two species arrive at a point where they have similar functional forms, but they have developed those similar forms via different evolutionary pathways. EX: bat and bird
64
Divergent evolution:
the process by which species develop different forms AND thereby form new species, all radiating from that common ancestor. is an example of adaptive radiation
65
Hardy Weinberg equilibrium:
p2 + 2pq + q2 = 1
| p+q=1
66
Kingdom Phylum Class Order Family Genus Species: of humans
| King Phillip Came Over From Great Spain:
K: Animalia P: Chordata C: Mammalia O: Primates F: Hominidae G: Homo S: Homo Sapiens
67
Autotrophs:
are capable of fixing CO2 and can therefore use CO2 as their carbon source for synthesizing organic molecules.
68
Heterotrophs:
cannot fix CO2 and therefore must ingest organic molecules such as carbohydrates as their carbon source
69
Fungi:
grow via long, intertwining branches called hyphae. Hyphae are haploid and a mass of
hyphae is called a mycelium.
70
Commensalism:
symbiosis in which one participant benefits and the other participant’s experience is neutral— neither beneficial nor harmful
71
Lichen
Symbiosis between fungi and algae.
72
Bacteriophages
Virus that infect bacteria. Have a head, a tail, tail fibers, can contain dna or rna
73
Envelopes viruses
Ex:cold virus or HIV, small spherical membranes surrounding a protein capsid and nucleic acid. Retroviruses always contain RNA and reverse transcriptase enzyme
74
Glomerulus:
a fenestrated capillary bed that strains the blood—allowing fluids, ions, and molecules the approximate size of glucose or smaller to pass through into Bowman’s capsule.
75
Proximal tubule:
Sodium is reabsorbed via active trasport,and glucose is reabsorbed via secondary active transport through a symporter. because water and solutes are reabsorbed in the same ratio, the filtrate remains isotonic
76
Descending loop of henle:
This section of the nephron is impermeable to salts, but very permeable to water.
Water therefore flows out of the filtrate and into the medulla, concentrating the urine.
77
Ascending loop of henle:
This portion of the loop is impermeable to water and actively transports ions out of the filtrate and
into the medulla.
78
Distal tubule:
regulates calcium, sodium and hydrogen concentrations. Recall that aldosterone stimulates increased sodium reabsorption at the DCT and the collecting duct
79
Aldosterone:
also causes reabsorption of Na+ out of the collecting duct via the insertion of Na+ channels, K+
channels, and Na+/K+ ATPases in the cells that line the collecting duct. The net effect = water
retention and increased blood pressure.
80
ADH:
acts on the collecting duct, making it permeable to water
The net effect = water retention and increased blood
pressure.
81
Path of air in respiration:
Mouth/nose -> pharynx -> larynx ->trachea ->bronchi ->bronchioles -> alveoli.
82
Tidal Volume:
the volume of air that enters and exits the lungs during an average, unforced respiration
83
inspiratory reserve volume (IRV) and
| an expiratory reserve volume (ERV).
This is the volume of additional air that can be exhaled or inhaled after a normal, unforced expiration or inhalation
84
Residual volume:
amount of air left in the lungs after a forced, maximal exhalation
85
Vital capacity:
the total volume of air the lungs can hold at maximum inflation, minus the residual volume.
86
Hemoglobin:
4 subunits, each with one heme, each heme holds one O2 molecule. 1 Hemoglobin=8 O molecules
87
Equation for CO2 dissolving in blood:
CO2 + H2O = HCO3- + H+
88
Sympathetic NS activity:
increases heart rate and blood pressure. “Fight or Flight.” Cell bodies located far from the effectors. Neurotransmitters-> acetylcholine at the ganglia, norepinephrine at the effector.
89
Parasympathetic NS activity:
decreases heart rate and blood pressure.“Rest and Digest.” Cell bodies located very close to, or inside, the
effector. Neurotransmitters: acetylcholine only, at both the ganglia and the effector.
90
Platelets:
Tiny membrane-bound drops of cytoplasm. They are sticky when exposed to injured epithelium and non-sticky to healthy epithelium. If they encounter injured epithelium, they release chemicals that activate other platelets and clotting factors.
91
Hematopoesis:
All blood cells develop from stem cells (undifferentiated cells) in the bone marrow;
92
Function of the Lymphatic system:
Gather excess interstitial fluid and return it to the blood; remove from the interstitial spaces proteins and other molecules too big to be taken up by the capillaries;
monitor the blood and lymph for infection
93
Where do lymphatic vessels drain?
into two main vessels, the right lymphatic duct and the thoracic duct, which both dump back into the blood stream by merging with large veins in the lower portion of the neck.
94
4 Characteristics of Neurons:
1) Are frozen in G0 phase (unable to divide)
2) Depend entirely on glucose for energy
3) Don’t require insulin for glucose uptake
4) Have very low glycogen; oxygen storage capability and thus require high perfusion (blood flow)
95
Sodium/potassium pump:
An ATP pump that actively transports 3 Na+ ions out of the cell and 2 K+ ions into the cell per cycle.
96
Voltage Gated Sodium Channels:
In their “open” state, they allow the rapid flow of sodium back into the cell.
97
Depolarization:
The opening of the voltage gated sodium channels causes a sudden spike in the membrane potential, from -70 mV to somewhere around +40 mV
98
Where is the threshold potential?
around -55mV
99
Where are electrical synapses found?
the retina, smooth muscle, cardiac muscle, and the CNS.
100
Acetylcholinesterase:
Specialized enzymes in the synaptic cleft must break down the neurotransmitter to interrupt its action. If this didn't occur, the NT's (often acetylcholine) would continue to signal.
101
Schwann cells and oligodendrocytes:
Schwann cells: PNS wrap neuron
| Oligodendrocytes: CNS wrap neurons
102
Ependymal cells:
classified as epithelial and neural: cells lining the
| cerebrospinal fluid cavities for support.
103
Sensory neurons: (afferent)
Receive sensory signals from sensory cells.
104
Motor neurons: (efferent)
Carry signals to a muscle or gland to respond to the stimulus. Synapses with "receptor" and "effector"
105
Interneurons:
Connect afferent and efferent neurons. They also transfer and process signals. The brain and 90% of all other neurons are interneurons.
106
Endocrine system:
release hormones into the internal fluids of the body (e.g., blood, lymph, etc.).
107
Peptides:
Water soluble
108
Anterior pituitary hormones: (are released by hormones coming from hypothalamus)
FSH, LH, ACTH, hGH, TSH and Prolactin
109
Posterior pituitary hormones: (are released by hormones coming from hypothalamus)
ADH and Oxytocin
110
What hormone does the parathyroid release?
PTH- Parathyroid hormone
111
What hormone does the pancreas release?
Glucagon; Insulin
112
Thyroid:
Calcitonin
113
Embryo/Placenta:
hCG (Human Chorionic Gonadotropin)
114
Steroids:
All are lipid soluble and are cholesterol derivatives.
115
Tyrosines:
Lipid soluble (which require a vesicle for transport)
116
Lipid soluble hormones: (do not require membrane receptor, can diffuse freely)
(which require a vesicle for transport) almost exclusively act by binding to a receptor on or inside the nucleus and influencing transcription; peptide hormones, by contrast, act at a variety of cell locations.
117
What is the 1 major important rule about hormones?
Hormones always act to return the system to homeostatic, or “normal,” conditions. They never cause a drift away from normal.
118
INSULIN:
When high blood glucose levels are detected, the body tells the pancreas to produce insulin which causes the cells to uptake glucose from the blood, decreasing the levels.
119
GLUCAGON:
When low blood glucose levels are detected, the body tells the pancreas to produce glucagon which stimulates the liver to break down glycogen to release glucose into the blood, raising the levels.
120
Increase CO2=low pH (acidic)
Decrease CO2=high pH (basic)
Describe how this affects BP:
If BP is increased, velocity of blood increases, allowing less time for CO2 to be dumped in blood, causing more basic blood.
121
What specific type of cell does not require insulin to uptake glucose?
NEURONS
122
What neurons are in the CNS?
Interneurons only
123
What neurons are in the PNS?
Somatic: voluntary, skeletal muscle and has sens and mot
Autonomic: involuntary, innervates cardiac muscle, smooth muscle, and glands. Has sens and mot
Sensory:
Motor:
Sympathetic:
Parasympathetic:
124
4 different substituents of an amino acid?
contains four different substituents, an –R group, a hydrogen, a carboxylic acid, and an amine. All can be synthesized from glyceraldehyde
125
Are most amino acids found in human body D or L?
L, oriented with COOH at top, -R on bottom, amine group will be on left in fisher projection
126
-R groups of amino acids determine what?
CHEMISTRY, and folding of proteins and how they will interact
127
How will a protein fold?
Hydrophobic –R groups fold INTO the protein core
(hydrophobic environment), and hydrophilic –R groups are more common on the surface of the protein (hydrophilic environment).
128
Zwitterion
A dipolar version of an amino acid wherein
positively and negatively charged functional
groups cancel one another out, resulting in a
neutral ion
129
Salt bridges:
Formed when acidic and basic –R groups undergo a neutralization reaction resulting in a salt.
130
What kind of resonance is demonstrated in a peptide bond?
BOTH the C=O bond and the C-N bond in a
| peptide bond have DOUBLE BOND character.
131
What molecules cleave proteins on carboxylic acid side of amino acids?
* Trypsin = arginine, lysine
| * Chymotrypsin = phenylalanine, tryptophan, tyrosine
132
How far apart are the hydrogen bonds in an alpha helix?
4 amino acids apart, including AA's participating in bonds. R groups are directed exactly away from the alpha helix cylinder
133
Beta sheets:
| EX: keratin, fibroin
H bonding between carbonyl oxygens and NH hydrogens.
ALL residues involved in hydrogen bonding!
Proline usually and end of row to induce 180 deg turn
134
The six types of interactions in teritary protein structures?
Hydrogen bonding, disulfide bonds, hydrophobic/hydrophilic interactions, Ionic interactions, van der wals forces, proline turns .
135
Quaternary proteins consist of:
Two alpha subunits and two beta subunits
136
Positive cooperativity:
Ligand affinity increases with the binding of each
subsequent ligand. In the case of hemoglobin, affinity for the first oxygen is relatively low, but increases for the second, third, and fourth oxygen to bind. This affinity remains in effect during offloading of oxygen at the tissues.
137
disulfide bonds:
Two oxidized cysteine residues form a disulfide (R-S-S-R) bond. This is the strongest type of protein folding interaction.
138
Salt bridges:
Formed when acidic and basic –R groups undergo a neutralization reaction resulting in a salt.
139
Solvation Layer:
A layer of water that surrounds a dissolved protein. The water molecules in this layer interact closely with each other and with the protein’s surface.
140
What aspect of a protein most affects the way it folds?
It's AA sequence
141
Name four protein denaturing agents?
▪ Acid
▪ Heat
▪ Urea
▪ Mercaptoethanol
142
Isoelectric focusing:
A gel is created with stable pH gradient. A
protein in a region of the gel with a pH lower than its isoelectric point will be positively charged (because it will be fully protonated) and so will move toward the negative cathode. Vis versa for High pH. As the protein moves through increasing pH in the gel, the protein’s charge will decrease until it reaches the pH of its pI, at which point it will become neutral. At this point the protein will cease to move through the gel, because it has no charge and so has no pull toward either electrode. This causes proteins to
form very sharp bands at the pH equal to each protein’s pI.
143
Electrophoresis:
Proteins are denatured, coated in negative charge uniformly, run through polyacrilamide gel from negative to positive, the smallest fragments will run the furthest.
144
Kinesins:
Move along microtubules from (—) to (+) end [center of cell to periphery; nerve cell body -> dendrite]
145
Dyneins:
Move along microtubules from (+) to (—) end [periphery to center of the cell; nerve cell dendrite -> cell body]
146
Relationship between catalysts and enzymes:
Enzymes (organic) are always catalysts, but catalysts can be enzymes or inorganic material. Both are used over and over without diminishing.
147
Enzyme classifications:
| Enzymes help reactions O T HILL (over the hill):
▪ Oxidoreductases = REDOX reactions
▪ Transferases = Transfer of a functional group (e.g., kinases, aminotransferases)
▪ Hydrolases = Hydrolysis
▪ Isomerases = Rearrangements (e.g., phosphoglucose isomerase [G6P F6P], epimerases)
▪ Lyases = AB A + B [cleavage/synthesis; NO H2O, NOT hydrolysis]
▪ Ligases = Addition or synthesis of LARGE molecules, usually ATP-dependent (e.g., DNA Ligase)
148
Enzyme substrate induced fit theory:
predicts that the active site’s empty structure is not an exact fit for the substrate, and may be rather nondescript. As the substrate begins binding the pocket, small but specific conformational
changes occur, such that the final shape and charge characteristics of the active site are not in place until the substrate is completely bound. This is the favored theory:
149
Enzyme substrate lock and key theory:
predicts that the active site of an empty enzyme is an exact fit for its substrate; the substrate is the key, and the enzyme active site is the lock. This model is not favored by scientists because it predicts a very rigid, inflexible active site. Energetically, this would be unfavorable, and sterically for many enzymes this would be unlikely or impossible
150
Cofactors:
A general term for any species required by an enzyme to function; coenzymes and prosthetic groups are both examples of cofactors.
151
Coenzymes:
Non-protein species NOT permanently attached to the enzyme but required by the enzyme to function.
152
Prosthetic group:
Non-protein species that ARE permanently attached to the enzyme and are required by the enzyme to function.
153
V-Max:
the rate of the reaction at saturation levels of substrate. This is the theoretical maximum rate of the
reaction, although in practice the reaction will never reach this velocity
154
Michealis menten kinetics equation:
V = Vmax[S]/(Km + [S])
155
Km
[S] @ ½Vmax
is the Michaelis constant, the substrate concentration at half Vmax. Relative measure of an enzyme’s affinity for its substrate. The magnitude of Km is INVERSELY proportional to substrate-enzyme binding affinity. The lower the Km, the stronger the binding affinity.
156
Lineweaver burke plots:
A double-inverse graph of the Reaction Rate (v inverted to 1/v) and substrate concentration ([S] inverted to 1/[S]) graph described above.
157
Competetive inhibition: (reversible)
Inhibitor binds at the active site; The inhibitor resembles the substrate in shape; the inhibitory effect can be overcome by increasing the concentration of the substrate.
• Vmax = NO CHANGE
• Km = INCREASES
158
Uncompetetive inhibition: (reviersible)
Inhibitor binds ONLY with the enzyme-substrate complex.
• Vmax = DECREASES
• Km = DECREASES
159
Non competetive: (reversible)
Inhibitor binds away from the active site and changes the shape of the enzyme. The inhibitor has an equal affinity for both the enzyme-substrate complex (E-S) and the enzyme (E).
• Vmax = DECREASES
• Km = NO CHANGE
160
Mixed inhibitor: (reversible)
Inhibitor has unequal affinity for the E-S and the E, favoring one over the other.
• Vmax = DECREASES
• Km = DECREASES if inhibitor = affinity for E-S over E
• Km = INCREASES if inhibitor = affinity for E over E-S
161
Irreversible inhibition:
Inhibitor binds covalently to the enzyme and/or the active site, disabling the enzyme for either a prolonged period of time, or permanently.
162
Feedback inhibition or negative feedback:
A specific type of non-competitive or allosteric
inhibition that applies to multi-step reactions, synthetic pathways, or cascades. One of the products
of a reaction later in the chain acts as an inhibitor for one of the enzymes earlier in the chain.
163
Zymogen
– An inactive enzyme precursor
164
Allosteric enzyme:
– Enzymes whose activity is influenced by the reversible, non-covalent binding of another
molecule
165
Carbohydrates:
monosaccharides = (CH2O)n ; polysaccharides = Cn(H2O)
166
Common disaccharides:
lactose = galactose + glucose (-linked)
maltose = glucose + glucose
sucrose = glucose + fructose
167
What occurs naturally in humans, D sugars or L sugars?
D sugars, NOT L sugars
168
Sugars: Aldoses-Glucose, ribose, deoxyribose
Ketoses- Fructose
Which of these are reducing?
Aldose sugars reduce (through the sugar becoming oxidized by reducing something else) by the aldehyde group.
169
Lipids:
Bio molecules, hydrophobic
170
triacylglycerol:
A lipid, glycerol molecule with three fatty acid tails bonded together by 3 esters. The forming of the esters is called SAPONIFICATION
171
Steroids:
All steroids are 4 membered ring strucutes, A B C D, listed from the ring closest to the OH group being A, and D being closest to the R chain
172
Prostoglandins:
Lipid mediators that have autocrine (self-target) and paracrine (target = cell in immediate
vicinity) functions throughout the body.
Produced and released throughout the body; NOT only in specialized glands.
Act locally, rather than traveling to a distant target via the bloodstream.
173
What lipids are amphipathic?
: fatty acids (carboxylic acid is polar), phospholipids (phospho group is polar), sphingolipids (oxygen and nitrogen are polar), and glycolipids (oxygens of the sugar are polar).
174
Gylcolosis:
Cuts up glycogen to make more sugars when needed.
175
Gluceogenesis:
Forms glucagon from free sugars for storage.
176
How is bond dissociation energy related to acids?
Stronger acid = smaller bond dissociation energy
| Weaker acid = Larger bond dissociation energy
177
Anaerobic respiration/fermentation:
When insufficient oxygen is available ( for muscles in extended exercise), glucose undergoes anaerobic fermentation with pyruvate acting as the final electron accepter
178
Where does crossing over occur?
Prophase I
179
Where does independent assortment occur?
Metaphase I
180
What type of transport is uptake of glucose from the gut
Secondary active transport
181
What muscle types contain gap junctions?
Only smooth and cardiac, not skeltal
182
Is ph more acidic in the inter membrane space or the matrix?
intermembrane space
183
Microtubules examples:
Spindle fibers, cell structure, cilia and flagella
184
Microfilaments:
Actin, responsible for protein transport
185
Physical digestion:
chewing (mastication), churning in stomach, and breaking of food into smaller pieces, including emulsification of fats by bile.
186
Heterotrophs:
Don't have the ability to “fix” carbon is the ability to capture carbon dioxide and integrate that
carbon into larger macromolecules
187
Chemical digestion:
all breakdown of food that involves the breaking of bonds through the use of digestive enzymes.
188
Liver function:
Manufactures bile
189
Gallbladder function:
Concentrates and stores bile, BUT DOES NOT PRODUCE IT.
190
Pancreas function:
secretes bicarbonate into the duodenum to neutralize the acidic chyme coming from the stomach, decreasing stomach to pH 6. The pancreas also secretes six pancreatic digestive enzymes. trypsin, chymotrypsin, pancreatic amylase, lipase, ribonuclease, and deoxyribonuclease.
191
name of the reaction by which amylase catalyses carbohydrate breakdown?
The breakdown of all nutrient macromolecules into their monomers is accomplished via hydrolysis.
192
What are the names of inactive enzyme precursors?
Zymogens are inactive enzyme precursors.
193
What are pepsin and pepsinogen?
Hydrolysis in the stomach is catalyzed by pepsin, which begins as pepsinogen.
194
Four stomach lining cell types?
Mucous neck cells, chief cells, parietal cells, G-cells.
195
Mucous neck cells:
Make and secrete mucus (into gastric pits, which lead to the stomach. lumen) The secreted mucus is alkaline, thus providing protection from corrosion due to the
extreme acidity of the stomach. NOTE: “Goblet cells” are mucus-secreting cells found in the linings of the intestines and respiratory tract. Don’t confuse them with mucous cells.
196
Chief cells:
Make and secrete the zymogen pepsinogen (into gastric pits/stomach lumen)
197
Parietal cells:
Secrete HCl (into gastric pits/stomach lumen). HCl is responsible for the extreme acidity (pH = 2) of the stomach and for the conversion of pepsinogen to pepsin, the active form of the enzyme.
198
G-cells:
Make and secrete gastrin. Gastrin is released into the blood (NOT into the gastric pits/stomach lumen) where it circulates back to the parietal and chief cells stimulating them to release HCl and pepsinogen thus further enhancing digestion.
199
The Liver:
Think of the liver as the “metabolic brain” of the human body. Here are a few key functions:
• Produces Bile (stored and concentrated in gall bladder)
• Filters the blood to remove toxins, drugs, metabolites, bacteria, etc.
• Produces blood plasma proteins, including albumin, prothrombin and fibrinogen
• Regulates amino acid levels in the blood.
• Produces cholesterol and lipoproteins and packages them for transport (LDL, HDL, etc.)
200
Role of the Liver in Glucose Metabolism:
In response to low blood glucose levels, alpha cells in the pancreas secrete glucagon.
Glucagon stimulates glycogenolysis in the liver—the breakdown of glycogen stored in the liver to form free glucose for release into the blood.
In contrast, high blood glucose levels stimulate beta cells in the pancreas to secrete insulin.
Insulin stimulates glycogenesis in the liver—the synthesis of glycogen for storage in the liver.
201
Insulin:
Insulin stimulates glycogenesis in the liver—the synthesis of glycogen for storage in the liver.
Insulin also stimulates the uptake of glucose from the blood into the cells. Finally, the liver converts lactate, glycerol, amino acids, and some TCA-cycle intermediates into glucose
202
what type of gland is the pancreas?
both an endocrine and an exocrine gland. (exocrine because of the digestive enzymes listed below and endocrine because of insulin and glucagon).
203
Trypsin and Chymotrypsin:
are both proteases that cleave peptide bonds at specific amino acid sequences
204
Pancreatic amylase:
catalyzes the hydrolysis of carbohydrates
205
Lipase:
catalyzes the hydrolysis of fats
206
Ribonuclease and deoxyribonuclease:
catalyze the hydrolysis of RNA and DNA
| respectively.
207
The Small Intestine:
The majority of all digestion and absorption occurs in the small intestine; digestion occurs primarily in the duodenum with absorption primarily in the jejunum and ileum. Contains villi and microvilli to increase surface area for max absorption. Contain lacteals for fat absorption, and blood vessel for protein and carb absorption.
208
The Large intestine:
Whenever you see “water absorption” or “vitamin absorption” THINK of the large intestine. In addition to absorbing vitamins from food, the large intestine also absorbs some vitamins produced by beneficial symbiotic E. coli bacteria that live in the large intestine (e.g., vitamin K, thiamin, riboflavin, and B12)
209
Where are carbs digested?
Start in mouth by salivary amylase, all digested by the time they get through small intestine. Broken down to small sugars and taken through blood to liver.
210
Where do proteins begin digestion?
Stomach, broken down completely by end of small intestine, taken through blood to liver.
211
Where does lipid digestion begin?
Small intestine, (duodenum) and is complete by end of small intestine. This is where they encounter bile (intersection of pancreas, liver and gallbladder).
212
Macrophages:
phagocytize pathogens and cellular debris. Phagocytosis by macrophages is non-specific and a type of innate immunity, but macrophages also present antigens from pathogens they consume for recognition by B and T cells, an aspect of acquired immunity
213
Neutrophils: (granulocyte)
Stain neutral pale pink. Neutrophils are phagocytes that are recruited to areasof infection and inflammation by chemotaxis. They live for only about 5 days, but are the mostabundant of all white blood cells. The pus created at a wound is mostly dead neutrophils
214
Basophils: (granulocyte)
the least common white blood cell. Their granules contain mostly histamine, which they release along with other chemicals when activated. These chemicals promote inflammation and are integral in the allergic response, so many associate basophils will allergies. Stain dark blue
215
Eosinophils: (granulocyte)
Stain a bright red. are recruited to areas of parasitic invasion, particularly multicellular parasites,
where they release their granules containing peroxidases and other enzymes that digest tissue.
This would destroy the pathogen but could also destroy host tissue.
216
Mast cells:
permanent resident cells within many tissues. They are activated by allergens and other antigens to release histamine and other chemical mediators. They are usually associated with severe allergic reactions, including anaphylactic shock
217
Dendritic cells:
professional antigen-presenting cells. They efficiently
phagocytize pathogens and present those antigens on their surface to stimulate other immune cells. Dendritic cells are white blood cells (leukocytes), but are not lymphocytes.
218
Natural killer cells:
recognize infected or cancerous cells and release cytotoxic granules that destroy the cell.
219
T-Cells:
lymphocytes that mature in the thymus and participate
| in cell-mediated immunity
220
B-cells:
lymphocytes that mature in the bone marrow and lymph
| tissues and participate in humoral immunity. B-cells produce antibodies, T-cells do not
221
Plasma cells:
formed when a B-cell binds its matching antigen and is activated (with the help of helper T-cells) to undergo mitosis.
222
Memory B cells:
A few cells will differentiate into memory B cells that remain in the body, allowing the immune system to mount a more efficient secondary immune response if there is a later infection by the same pathogen
223
Helper T cells:
T-cells that “help” other immune system cells, such as B-cells and cytotoxic T-cells, to perform their function. The way they “help” other cells is usually to secrete chemicals, such as cytokines, that activate (i.e., “turn-on”) functions or activities in the cell that is being “helped”
224
Suppressor T cells:
suppress the body’s own immune system—which helps prevent severe allergic reactions or autoimmune
disease and aids in turning off an immune response once an infection has been eliminated.
225
Cytotoxic T cells:
target infected and cancerous versions of the body’s own cells and destroy them
226
Spleen:
Somewhat analogous to a lymph node that filters blood instead of lymph; high concentration of leukocytes (WBCs) and platelets; storage of a considerable amount of blood that can help combat hemorrhagic shock; breaks down and recycles parts of old erythrocytes
(RBCs).
227
Thymus:
Location where T-lymphocytes (a.k.a. T cells) acquire immunocompetency, differentiate, and mature.
228
Lymph nodes:
High concentration of B- and T-lymphocytes. Filters blood for pathogens
229
innate immunity;
All forms present at birth, not acquired in any way.
230
Acquired immunity:
A specific response to one particular virus, bacteria or other pathogen based upon prior exposure. There are two types of acquired immunity: humoral and cell-mediated.
231
Hummoral immunity:
Think B cells and anitbodies. If an antigen binds to a B-cell’s antibody, the B-cell will undergo differentiation into a plasma cell and a memory B-cell. Primary and secondary response are in this category, the first exposure to an antigen(primary) and the second exposure or anything thereafter is secondary.
232
Cell mediated immunity:
Think T cells. they are “tested” in the thymus against the host’s own membrane proteins (called “self-antigens”). All T-cells matching a self-protein are destroyed, leaving only cells that will recognize invaders. If they pass test they will then differentiate into a diff type
233
MHC proteins. Major Histocompatability Complex:
Antigen presentation is the process by which a cell that has engulfed an antigen or microbe, (via receptor-mediated endocytosis or phagocytosis) takes protein segments of that microbe, and “presents” them on MHC (Major Histocompatability Complex) proteins embedded
in its own cell membrane. This makes the engulfed antigen/foreign proteins available for other cells
to “see.”
234
Order of skin layers:
Epidermis (mostly dead skin cells), Dermis (blood vessels, hair follicles, sebaceous glands). Dermis is considered connective tissue.
235
Blood vessels ____ to release heat and ____ to retain it.
Dilate to release, constrict to retain
236
Order of cells in muscles, large to small:
Fascicles, are bundles of muscle fibers (considered single cells), around each fiber is a sarcolemma, and inside each muscle cell are many nuclei. The rest of the cell is filled with myofibrils, which are composed of actin and myosin fibers, which are connected repeatedly and called sarcomeres. MUSCLE CELLS HAVE SARCOPLASMIC RETICULUM INSTEAD OF ER.
237
Main component of thick filaments?
Myosin, a motor protein. Default position and low energy position is BENT
238
Order of a muscle contraction:
```
Myosin heads have a high affinity for actin and bind it unless the actin binding sites are blocked by
tropomyosin, which like troponin is made up of actin and is a thin filament. A bands stay same during contraction. I bands shorten. H zone shortens (distance between ends of actin fil).
ATP hydrolysis (ATP ADP + Pi) provides the energy required to straighten, or “cock” these myosin heads into their high-energy, straight position.
```
239
How does calcium cause contraction within a muscle cell system?
When calcium is released from the sarcoplasmic reticulum it binds to troponin, releasing the “clamp” from tropomyosin and freeing the binding site. When they relax back to their bent position while still bound this is the power stroke. After the power stroke, ATP binds to the myosin head again facilitating its release from the actin filament.
240
What impact would lack of ATP or Ca2+ have on muscle contraction?
▪ If no ATP is present, the myosin heads cannot detach from actin and the muscle will be stuck in a contracted position called “rigor.” This is what occurs during “rigor mortis”.
▪ If no Ca2+ is present, we do NOT get rigor, but the inability to contract (a.k.a., “flaccidity”).
241
How do skeletal muscles store glycogen?
Myoglobin is basically one subunit of a hemoglobin molecule, capable of holding one O2 molecule. Mature
(differentiated) skeletal muscle cells are suspended in Go phase and do not divide (similar to neurons).
242
How does cardiac muscle contract?
Same way as skeletal, with myosin filaments and actin
243
Characteristics of cardiac muscle:
Gap junctions, uses myoglobin like skeletal, continue dividing after differentiation
244
Features of smooth muscles:
does not contain sarcomeres, still uses myosin and actin but with different proteins involved in sliding mechanism,
245
3 types of bone cells:
Osteocytes: Mature bone cells surrounded by a mineral matrix.
▪ Osteoclasts: Bone cells that break down and resorb bone matrix, releasing the component
minerals (Ca2+ and P) back into the blood.
▪ Osteoblasts: Immature bone cells that secrete collagen, organic compounds, and minerals
forming a bone matrix around themselves. Once they are completely enclosed by matrix, they
differentiate into osteocytes
246
2 hormones that regulate bone maintenece:
parathyroid hormone (PTH) and calcitonin. Parathyroid stimulates osteoclasts (when more calcium is needed by breaking bones down) and calcitonin inhibits osteoclasts.
247
3 joint types:
1) Fibrous (skull bones)
2) Cartilaginous (pubic symphysis, intervertebral discs)
3) Synovial (knee, elbow, etc.)
248
Anatomy of a long bone:
```
Two epiphyses (bulbous ends) cushioned by cartilage; the ends are filled with spongy bone and the shaft in between is made of compact bone; the center is a
hollow cavity filled with yellow bone marrow
```
249
Hydroxyapatite:
is an inorganic compound of calcium, phosphate, and hydroxide. It is the
mineral matrix responsible for a bone’s strength and is the form in which most all of the body’s
calcium is stored.
250
Sperm storage and pathway:
They are produced in the seminiferous tubules of the testes and move to the epididymis, where they are nurtured, fully matured, and stored until ejaculation. The vas deferens is a duct that connects each testicle with the urethra. Beginning at the epididymis, it leads up the inside of the scrotum, into the pelvic cavity, past the seminal vesicles, through the prostate gland, and
empties into the urethra before the urethra enters the penis
251
Acrosome:
a membrane-bound structure on the tip of the head of each sperm. The acrosome contains hydrolytic enzymes that break down the otherwise impenetrable coating
around the ovum.
252
Are Benzenes or aromatic compounds polar or non polar?
Non polar, so they are hydrophobic.
253
In electrophoresis, what type of charge do we give the molecules before starting?
We give them a negative charge, and they then move towards a positive end.
254
Totipotent cells:
Cells can give rise to all of the cell types in the body, including extraembryonic or placental cells. Embryonic cells within the first few cell divisions after
fertilization are the only cells that are totipotent.
255
pluripotent cells:
Cells can give rise to all of the cell types that make up the body, but not extraembryonic cells. Undifferentiated embryonic stem cells are considered pluripotent.
256
multipotent cells:
Cells can develop into more than one cell type, but are further differentiated and more limited than pluripotent cells; adult stem cells and cord blood stem cells are
considered multipotent
257
Ectoderm:
epidermis, nails, tooth enamel, lens of the eye, pituitary gland, central, peripheral and autonomic nervous systems.
258
▪ Mesoderm:
dermis, muscle, bone, connective tissues, kidneys, genitalia and most internal organs EXCEPT the liver and pancreas.
259
▪ Endoderm:
the entire digestive tract, thyroid, parathyroid, urinary bladder, the lining ONLY of the lungs, the liver and pancreas.
260
What is high estrogen/progesterone levels associated with?
the thickening of the uterine lining
261
Order of protein unfolding? folded to unfolded
Natively folded -> molten globular -> pre- molten globular -> unfolded
262
What is a caspase?
They are proteases which cleave proteins at cisteins, that trigger apoptosis. Are found in most normal cells.
263
Column chromatography, do bigger or smaller molecules travel through faster?
Bigger faster, smaller slower because they get hung up.
264
A palindrome :
Reads same from 5' to 3' on one strand as they do from 5' to 3' on the complementary strand.
265
The dynamic steady state:
“Dynamic Steady State” describes the ability of living things to maintain a constant, steady internal environment that is NOT in equilibrium with its surroundings. For example, your body temperature remains a fairly constant 98.6F, and yet the room you
are in right now is probably about 75F
266
Substrate level phosphorylation:
Formation of ATP from ADP in which the source of
the necessary phosphate is a phosphate bound to another molecule (i.e., the “substrate”).
To proceed, this process MUST be coupled to an exergonic reaction.. Normally in cytosol but also in matrix of mitochondria during citric acid cycle.
267
Oxidative phosphorylation:
Formation of ATP out of ADP and Free Organic Phosphate (Pi) by harnessing the energy of the proton gradient across the inner mitochondrial membrane. This proton gradient is created as a result of coupling the oxidation of highenergy molecules such as NADH and FADH2 to the pumping of protons. Only in mit matrix.
268
Hydrolysis of ATP:
ATP + H2O ADP + Pi + energy. ATP hydrolysis is almost always coupled to another reaction or process, such that the free energy released can be utilized to drive another reaction or do work (e.g., cocking
the myosin head).
269
LIst the most common molecules involved in redox reactions:
: NADH/NAD+, NADPH/NADP+ FADH2/FAD, FMNH2/FMN, semiquinone (an FMNH radical), ubiquinone, or cytochrome
270
Aerobic respiration:
uses oxygen as the final electron acceptor, involves all the reactions involved in the citric acid cycle and electron transport, Humans use aerobic respiration to generate the vast majority of our ATP.
271
Anerobic respiration:
Anaerobic respiration uses a molecule other than oxygen to accept electrons. will typically refer to fermentation, using glycolysis in the absence of oxygen, or the lactic acid cycle in muscles, we use anaerobic respiration in our muscles during exercise that results in a buildup of lactic acid.
272
Obligate vs faculative aerobes:
obligate aerobes must use aerobic respiration and cannot survive without oxygen, “Facultative” implies that the organism will use whichever respiration is available. So if oxygen is present, the organism will use aerobic respiration, and if oxygen is absent, the organism will use anaerobic respiration.
273
Obligate vs faculative anerobes:
obligate anaerobes must use anaerobic
| respiration and cannot survive in the presence of oxygen. Faculative can do both but prefer anerobic in this case.
274
Glycolysis breaks down glucose to form _____ with the production of __ ATP:
Pyruvate, 2. Pyruvate then either goes to anerobic or aerobic respiration.
275
Glycogen phosphorylase:
removes glucose residues from the reducing ends of glycogen polymers Glucose-1P
276
Phosphoglucomutase:
converts Glucose-1P Glucose-6P
| G-6P is then funneled into the 2nd step of GLY
277
In the muscles and kidneys, hexokinase:
converts Fructose Fructose-6P
| F-6P is then funneled into the 3rd step of GLY
278
What are the three steps of glycolysis that occur in the liver:
1) Fructokinase converts Fructose Fructose-1P
2) Fructose-1-phosphate aldolase converts Fructose-1P Glyceraldehyde-3P + Dihydroxyacetone-P (DHA-P)
3) Triose phosphate isomerase converts DHA-P Glyceraldehyde-3P
(GA-3P is then funneled into the 5th step of GLY)
279
Ethanol fermentation:
(primarily yeast, a few bacteria) Ethanol is produced and is the final electron acceptor. Ethanol fermentation is unique compared to lactic acid fermentation in that the
carbon skeleton changes. Pyruvate (3C) is broken down into ethanol (2C) and CO2.
280
Lactic acid fermentation:
In lactic acid fermentation, lactate is produced and is the final electron acceptor. Fermentation is IMPORTANT because it regenerates NAD+ so that glycolysis can continue. NAD+ regeneration is necessary for both human fermentation during oxygen debt and yeast/bacterial fermentation
281
Gluceogenesis:
Conceptualized as the reversal of glycolysis to produce glucose from pyruvate. : Gluconeogenesis = LIVER, fasting, and the need to increase blood sugar.
282
Retrograde trafficking:
Backwards, from outside cell to golgi to ER
283
Endonuclease:
Exonuclease:
Cuts DNA somewhere in the middle of the strand.
| Starts on the ends of DNA and chews up towards mid
284
Glucocorticoids:
have a “glucagon-Like” effect on metabolism (e.g., stimulating gluconeogenesis, glycogenolysis, and fatty acid oxidation). Glucocorticoids also reduce
inflammation.
285
Catecholamines:
Dopamine, Epinephrine, and Norepinephrine. Dopamine is a CNS neurotransmitter; Epinephrine (Adrenaline) and
Norepinephrine (Noradrenaline) are the two
metabolic hormones.
286
What are the three metabolism hormones?
Insulin, Glucagon, glucocorticoids, catecholamines, T3 & T4
287
T3 and T4 hormones:
: These thyroid hormones increase
basal metabolic rate; both are secreted by the
thyroid in response to TSH from the anterior
pituitary.
288
How many carbons are cleaved off in each round of B oxidation of lipids?
2 carbons. To determine how many rounds of oxidation is needed for even numbered chains, subtract 1 and divide by 2, for odd chains subtract 1, divide by two and then subtract 1 more.
289
Ketone bodies:
Acetone (no energy value), Acetoacetate (energy), and 3-Hydroxybutyrate (energy)
• Formed by the liver during prolonged fasting periods as byproducts of increased fatty acid metabolism. Two of the three can be used for energy during fasting periods by
the heart and brain. Ketone bodies CANNOT be used by the liver during fasting because it lacks a necessary enzyme.
290
Where are lipids metabolized for energy, synthesized, and
| elongated and modified?
Metabolized: in the mitochondria
Synthesized: in the Cytosol
Elongated and Modified: in the Smooth ER
291
Protein metabolism:
Most amino acids can be broken down into either pyruvate or acetyl-CoA and fed into the Citric Acid Cycle. The remaining amino acids can be transformed into various other Citric Acid Cycle intermediates
292
Transamination: (a key step in protein metabolism)
A key step in protein metabolism for energy is transamination of amino acids—or the exchange of an amine group on one molecule for a carbonyl group on another
293
Glutathione:
the most important antioxidant in counteracting the damaging impact of the peroxide and radical
byproducts of oxidative respiration.
294
The Pentose PHosphate Pathway (PPP):
When you see PPP THINK: PPP = 1) NADPH synthesis and 2) Ribose-5-Phosphate (R5-P).
295
NADPH:
is an important reducing agent (NADPH NADP+) used during “Reductive Biosynthesis”—a general term referring to a large number of reactions used to synthesize fatty acids and sterols. NADPH is also necessary for the production of Glutathione
296
R5-P:
is used to synthesize nucleotides. It is the oxygen-bearing ring of all nucleotides, including
the famous deoxy-ribo-nucleic acid.
297
Acetyl- CoA:
The first substrate of the Citric Acid Cycle. Its metabolic origin is most often thought of as a pyruvate from glycolysis converted to Acetyl-CoA by the PDH Complex (carbohydrate origin). However, Acetyl-CoA is also the primary product of the -oxidation of fatty acids (lipid origin), and one of the products of amino acid metabolism (protein origin).
298
What are the total number of molecules produced in glycolysis?
Overall, glycolysis produces two pyruvate molecules, a net gain of two ATP molecules, and two NADH molecules.
glucose + 2 NAD+ + 2Pi + 2ADP 2 pyruvate + 2ATP + 2NADH + 2H+
299
What are the total number of molecules produced in the krebs cycle?
Because for each glucose molecule there are two pyruvic acid molecules entering the system, two ATP molecules are formed (1 per pyruvate). Also during the Krebs cycle, the two carbon atoms of acetyl-CoA are released, and each forms a carbon dioxide molecule.
300
What is substrate level phosphorylation?
is the process by which a phosphate group is transferred to ADP or GDP from a phosphorylated intermediate. The Citric Acid Cycle uses substrate level
phosphorylation
301
Oxydative phosphorylation:
occurs in ATP synthase in the electron transport
chain. This process combines ADP and inorganic phosphate to generate ATP through the
generation of a proton gradient by transporting electrons.
302
How many protons are needed to generate an ATP molecule at the ATP synthase molecule in the ETC?
To generate one ATP molecule, 3 protons are needed. This means that every NADH generated will result in 3 ATPs, and every FADH2 will generate 2 ATPs.
303
How may ATP are produced per glucose in overall cellular respiration process?(glyc, Kreb, ETC)
36 ATP
304
Uncoupling in oxidative phosphorylation:
: It may be said that Drug X “uncouples” the ETC or the electrochemical gradient from oxidative phosphorylation. This means the gradient is no longer directly driving ATP production at the ATP synthase. For example, this could be because a drug inserted proton channels into the inner mitochondrial membrane. The ETC would continue to pump protons, but because protons have an alternate route back into the matrix, the two processes would no longer be directly or fully “coupled.”
305
Allosteric control:
When the product in a metabolic reaction builds up, it will interact more often with the enzyme that catalyzed the reaction, eventually inhibiting it from producing more product. Kind of like self shut off. Allosteric regulator molecules always binds AWAY FROM THE ACTIVE SITE. In other words, the effect is a change in the enzyme itself, NOT inhibition by competing with the substrate for the active site.
306
What are some characteristics of the metabolism during the well fed state?
• High insulin levels; low glucagon levels
• High relative rate of anabolism (vs. catabolism)
High rate of glycogen synthesis
High rate of fatty acid synthesis
307
What are some characteristics of the metabolism during the fasting state?
* High glucagon levels; low insulin levels
* Higher relative rate of catabolism (vs. anabolism; reversal of the well-fed state)
* Glycogenolysis = Immediate increase; Gluconeogenesis = Delayed increase (~12 hrs.)
308
What are some characteristics of the metabolism during the starvation state?
* VERY HIGH glucagon and epinephrine levels
* VERY HIGH rate of gluconeogenesis
* High rate of fatty acid oxidation, resulting in ketone bodies and acidosis
309
How does exercise molecule use change with duration?
the main fuel is glucose from the glycogen stores (switching from oxidative use of glucose to lactic acid fermentation during prolonged exercise); if exercise continues even longer (i.e., endurance athelete) the muscles must use only fatty acids.
Opposite for heart, it uses fatty acids when in well fed state.
310
What are the three hormones that help regulate body mass?
Leptin, Ghrelin, and Orexin
311
Differences between anabolism and catabolism:
Anabolism is the opposite of catabolism and is more often referred
to as synthesis. Anabolic processes construct larger macromolecules out of smaller precursors, while
catabolic processes breakdown macromolecules into smaller precursors or monomeric units.
312
"Non template" Fatty Acid Synthesis:
Occurs primarily in the cytosol of liver cells.
• Fatty-Acid synthesis is always the construction of 16-carbon palmitic acid, the only fatty acid the human body can synthesize from scratch. This occurs in the cytosol. Other forms of lipid synthesis, such as synthesis of phospholipids and steroids, occurs on the smooth ER.
313
Prostoglandin:
Type of hormone that only a lipid can secrete.
314
Reducing sugar:
Hemiacetal is needed. EX: Aldose
315
Euchromatin:
The chromatin that you use, or that is expressed.
316
Heterochromatin:
chromosome material of different density from normal (usually greater), in which the activity of the genes is modified or suppressed.
317
Fatty acid is comprised of:
a long hydrocarbon tail, and a head consisting of a carboxyl group
318
Oxidoreductase:
an oxidoreductase is an enzyme that catalyzes the transfer of electrons from one molecule to another. For redox reactions
319
Topoisomerase:
are enzymes that participate in the overwinding or underwinding of DNA
320
Ligase:
Most active on lagging strand, seals the nicks after the RNA primers are removed and repaired by DNA polymerase.
321
What nucleotide polymer is used as a template during homologous recombination?
The sister chromatid, because it is not damaged
322
Participant observation:
requires researcher to directly participate in the social phenomena being studied.
323
Symbolic racism:
Someone beleives that racism is wrong but do not see racism as a significant institutional problem in society since the 1960s.
324
Jim Crow Racism:
Institutional racism,
325
"second shift"
a concept used within the conflict theory perspective to explain the unequal division of labor in the household between women and men.
326
Lateral geniculate nucleus vs medial geniculate nucleus:
Lat: Vision processing
Med: Audio processing
327
The big 5 factor model of personality:
The Big Five personality traits, also known as the five factor model (FFM), is a model based on common language descriptors of personality. ... The five factors have been defined as openness to experience, conscientiousness, extraversion, agreeableness, and neuroticism, often represented by the acronyms OCEAN or CANOE.
328
The facial feedback hypothesis:
suggests that the physical expression of an emotion also activates the experience of tht emotion. If you express happiness, you will become happy
329
Valence:
Describes the inherent attractiveness or aversiveness of a stiulus, event or situation. attractive stimuli have positive valence and aversive stimuli have negative valence.
330
Heterochromatin:
Tightly bound chromatin, (DNA), can be due to methylation. Unusable due to this.
331
Euchromatin:
Usable DNA because it is loosely bound
332
Aldosterone fuction:
Aldosterone is released from the adrenal cortex in response to low blood pressure. Its primary function is to increase sodium reabsorption in the distal tubule and collecting duct. Aldosterone upregulates the sodium-potassium pumps along the lining of the nephron, pumping three sodium ions OUT of the nephron lining (and toward the blood) for every two potassium ions it pumps IN (toward the nephron and away from the blood).
333
What effect does lactose have on the body:
When lactose is present, it binds the lac repressor, causing the repressor to dissociate from the lac operon, and thereby allowing transcription of the proteins required to metabolize lactose
334
Function of Rybozime:
catalyze the polymerization of amino acids into peptides,
335
Diff between aldosterone and ADH?
look up
336
What is physiological temperature in Kelvin?
310 degrees
337
Does posterior pituitary synthesize hormones?
NO! It receives them from the hypothalamus and stores and releases many. IT interacts directly with neurons of the CNS.
