vert phys exam 1 Flashcards

(266 cards)

1
Q

acclimatization example

A

at high altitude with low pO2, more BPG and RBCs to carry oxygen

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2
Q

positive feedback ex

A

blood clotting;
blood vessel injury releases chemicals that activate platelets and cause coagulation
activated platelets release more chemicals and attract more platelets to injury site

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3
Q

autocrine regulation

A

chem. regulators affect same cells as produce them

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4
Q

physiology

A

study of functioning organisms and how organisms function
structure determines function, following laws of chem and phys

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5
Q

EC fluid - interstitial =

A

plasma volume

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6
Q

plasma vol + EC fluid =

A

interstitial fluid volume

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7
Q

plasma vol + EC fluid =

A

interstitial fluid vol

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8
Q

homeostatic mechanisms EX

A

shivering

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9
Q

epithelial cell function

A
  1. form boundary between compartments
  2. selectively permeable to ions and organic molecules
    - basolateral surf rests on basement membrane
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10
Q

steady state value that body maintains

A

set point

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11
Q

set point

A

steady state value that body maintains

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12
Q

location of internal pacemaker that sets biological rhythms

A

suprachiasmatic nucleus of the brain

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13
Q

suprachiasmatic nucleus of the brain

A

location of internal pacemaker that sets biological rhythms

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14
Q

endocrine control EX

A

heart rate increases from epinephrine release by adrenal medulla into bloodstream

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15
Q

4 cell types

A

epithelial, nerve, muscle, connective-tissue

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16
Q

homeostatic variable

A

in steady state of DYNAMIC CONSTANCY that is regulated to remain near a stable set point value

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17
Q

feed forward regulation

A

smell of bad food triggers the gag reflex
Smell/odor receptors trigger response in digestive sys
prepare stomach for arrival of food before it comes
saliva, churning, produce acid

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18
Q

steady state EX

A

upon entering a hot room, begins sweating
continued sweating keeps body temp stable

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19
Q

ID the EFFECTORS -
eating salt-rich meal increases blood volume and pressure, stretching vessel walls
nerve signals sent to brainstem stimulate Changes in hormonal/neural signaling.
heart rate slowed, blood vessel walls relax, kidneys increase salt exerted in urine
BP returns to normal

A

heart, blood vessels, kidney

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20
Q

ligand

A

molecule/ion that binds protein

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21
Q

A solution containing proteins of a particular type is exposed to the same concentrations of ligands X and Y, but the percent saturation of molecule X is greater than the percent saturation of molecule Y. why?

A

soon protein has a higher affinity for ligand X

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22
Q

increase temp of chem rxn

A

increase forward and reverse run rate

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23
Q

products of glycolysis under anaerobic conds

A

2 ATP, 2 H2O, 2 lactate

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24
Q

krebs cycle

A

generates ATP directly by substrate level phosphorylation

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25
RDS in metabolic path
slowest reaction, subject to end-product inhibition
26
true of fatty acid synthesis
begins with acetyl coenzyme A (coA) occurs in cytosol requires more energy than is produced by catabolism of same fatty acid results in even # of carbon atoms only \enzymes that synthesize fatty acids are found separately from enzymes that catabolize
27
muscle cell types
skeletal, cardiac, smooth
28
connective tissue cells
form ECM (fibers and collagen)
29
tissues
aggregates of differentiated cells with same type
30
body fluid compartments
intracellular fluid 67% plasma: part of blood which cells are suspended interstitial
31
EC fluid
interstitial fluid and plasma
32
why is there homogeneous solute composition in EC fluid?
EC fluid = interstitial + plasma Because of exchanges, concentrations of dissolved substances are identical in the plasma and interstitial fluid, EXCEPT for protein concentration (higher in plasma)
33
Compartmentalization
achieved by barriers - plasma membranes surround each cell, separate the intracellular from the extracellular fluid - 2 components of extracellular fluid— interstitial fluid and plasma—are separated by blood vessel walls.
34
homeostasis
1. state of dynamic constancy 2. stability of variable achieved by balancing input and output (not magnitudes) 3. Traits fluctuate within a predictable and often narrow range. 4. When disturbed out of normal range, restored to normal. 5. dynamic process regulates adaptive responses of body to changes in environ - require sensor to detect environ change - require compensatory mechs - achieved by expenditure of energy
35
compensatory mechanisms
restore homeostasis/set point
36
body temp as control sys EX
1. person at norm temp into cold 2. person loses heat to ext. enviro bc cold outside 3. compensation: chem rxns produce heat at rate = rate heat loss 4. blood vessel narrow and restricted, reducing blood flowing thru skin, decreasing heat loss from warm blood across skin into environ 5. body undergoes no net change and remains about constant; steady state - control sys operates around set point; maintainence
37
steady state
system where a variable is not changing but in which heat/energy must be added continuously to maintain stable, homeostatic condition NOT equilibrium (no input of energy req'd to maintain constant) ALL homeostatic control sys operate around a set point
38
negative feedback
thermoregulation a change in variable being regulated brings response that moves opposite the initial change towards the original point. corrective resp. after steady state perturbed
39
Negative feedback EX
product formed from substrate --> product reaction by an enzyme negatively feeds back to inhibit further action by enzyme (ATCase; ATP) as ATP accumulates, it inhibits the activity of enzyme and production slows down
40
resetting set points
FEVER; set point for body temp has been set higher and body responds by shivering to generate heat
41
feedforward regulation
improves the speed of body homeostatic response and minimizes fluctuations of regulated variable (reduces variation from set point) using environmental detectors/learning CHANGES IN REGULATED VARIABLES ARE ANTICIPATED/PREPARED FOR BEFORE THEY OCCUR
42
changes in regulated variable are anticipated/prepared for before they can occur improves speed of homeostatic response
feedforward regulation
43
feedforward regulation of temp
temp-sens neurons in skin monitor temp outside when its cold out, neurons detect change and relay info to brain which signals blood vessels/muscles resulting n heat conservation and increased heat production COMPENSATORY thermoregulation is ACTIVATED BEFORE colder outside temps can cause a decrease in internal boy temp
44
reflexes (control sys)
specific involuntary built-in response to stimulus can be automatic or learned/acquired from practice
45
specific involuntary built-in response to stimulus can be automatic or learned/acquired from practice
reflex
46
reflex arc mediation
stimulus acts on receptor and produces signal to be relayed to integrating center. signal travels along AFFERENT pathway to integrating center output is sent to EFFECTOR which acts along efferent pathway - if effector response causes decrease in stimulus trigger, then reflex leads to negative feedback and typical homeostatic control
47
stimulus
detectable change in environ
48
local homeostatic responses
initiated by change in environment/stimulUs, induce alteration of activity with NET EFFECT OF COUNTERACTING STIMULUS
49
stimulus/change in environment causes change in activity met by response with net effect of counteracting the stimulus
local homeostatic response - result from stimulus - local area resp. - nor nerves/hormones directly involved
50
hormones
chem. messenger that communicate and use the blood as a delivery sys for target
51
NTs
chem messengers released from neurons ending on other cells and diffuse thru EC FLUID separating neuron from its target NOT released into blood like hormone
52
paracrine
local communication between neighbor cells - NTS
53
adaptation
characteristic that favors survival in specific environments - homeostatic control systems are inherited and allow individuals to adapt to environ changes
54
acclimatization
prolonged exposure to environmental change = improved functioning of already existing homeostatic system reversible
55
adaptation/acclimatization EX
sweating in heat day 1: expose to 30 mins of heat and make exercise. body temp increases, sweating begins sweating is mechanism for increasing heat loss from body so body temp doesn't rise vol sweat measured day7 - subject begins to sweat sooner and much more profusely than day1. as consequence, body temp does NOT increase as much. subject ACCLIMATIZED to heat - undergone BENEFICIAL CHANGE INDUCED BY REPEATED EXPOSURE AND NOW BETTER ABLE TO RESPOND - reversible: if exposure stops, subject reverts to preacclimatized values
56
sweating
adaptation allows heat loss from body to minimize an increase in body temp in hot environments
57
cause of acclimatization
increase in number, size or sensitivity of 1+ cell types in homeostatic control system for response to exposure
58
biological rhythms
add an anticipatory comp. to homeostatic control like feedforward mechanism without detectors allow homeostatic mechanisms to be utilized automatically by activating when a challenge is likely to occur but before it does occur
59
an anticipatory comp. for homeostatic control like feedforward mechanism without detectors
biological rhythm
60
EX of biological rhythms
1. body temp increase prior to waking up so metabolic pathways can operate more efficiently 2. during sleep, metabolism slower than awake so body temp decreases
61
cause of biological rhythm
environ factors do NOT drive rhythm but provide timing cues for entrainment (set the rhythm)
62
total body balance
depends on relative rates of net gain/loss to body pool concentration depends on total amount of substance in the body and exchanges of substance within the body
63
total body balance depends on
1. relative rates of net gain/loss 2. pool concentration/total amount of substance in the body 3. exchanges of substance within the body
64
3 states of total body balance
1. loss exceeds gain: total amount substance is decreasing = negative balance 2. gain exceeds loss: total amount of substance in body is increasing = Positive balance 3. gain equals loss = stable balance
65
body balance EX
Calcium ions conc [Ca] in EC fluid the control system for balancing Ca targets the intestines and kidneys so amount of Ca absorbed from diet is balances with excretion during childhood, net balance Ca is + and deposited in growing bone later, Ca released from bones and lost in urine (rate of Ca loss exceeds intake so balance is negative)
66
homeostasis requires
energy to expend compensatory mechs sensor to detect environ change
67
Case study: A hot day
body temp increase, heat production decrease and heat loss increases sweating caused EC fluid levels to decrease eventually, fluid levels decrease so much that blood available to be pumped from heart decreased. IF EC FLUID DECREASES, BP DECREASES. sweat from EC fluid. more sweating and losing water (sweat is dilute EC fluid), more concentrated EC fluid is
68
sweat
from the EC fluid more dilute than EC fluid bc more H2O than ions is secreted more sweating = more concentrated EC fluid (saltier decrease EC fluid, BP decrease
69
prokaryotes
bacteria, lack membranous organelles
70
plasma membrane
limiting barrier, regulate passage, link adjacent cells by junctions and anchor cells to ECM double layer of lipid molecules with embedded proteins
71
largest intracellular fluid comp
cytoplasm/cytosol
72
phospholipid bilayer
plasma membrane amphipathic random lateral movement of lipids and proteins bc lack of bonds characteristic flex and fluidity
73
cholesterol
slightly amphipathic bc polar hydroxyl close association limits the ordered packing of fatty acids no cholesterol = tightly packed, less fluid MAINTAIN IM FLUIDITY
74
Integral proteins
amphipathic, move laterally, associated w membrane most are TRANSMEMBRANE form channels
75
Transmembrane proteins
integral proteins form channels
76
peripheral proteins
NOT amphipathic at membrane surface, cytosolic surface and bind polar regions assoc. w CYTOSKELETAL shape and mobility
77
fluid mosaic model
plasma membrane is lipid bilayer mosaic of membrane proteins that are free to move in a sea of lipids
78
junctions
provide barrier to movement of molecules between cells form tissues
79
integrins
transmembrane protein organizes cells into tissues by binding to ECM proteins and linking adjacent cell membranes
80
transmembrane protein organizes cells into tissues by binding to ECM proteins and linking adjacent cell membranes
integrin
81
desmosome
between 2 adj. cells structural support and integrity - characterized by accumulation of protein dense plaques along cytoplasmic surf of membrane - anchoring proteins to bind cadherins of adj. cell - bind to IM filaments - connect w integrins - adhesive junctions, hold adj. cells firmly together - in areas of mechanical stress, give stability - contains cadherins - keratin filaments anchor
82
feature between 2 adj cells that provides structural support/integrity accumulation of protein dense plaques on cytoplasmic surf
desmosome
83
desmosome dense plaques
anchoring proteins for cadherins extend from 1 cell into EC space to bind w/ cadherins of adj. cell - disk shape membrane.
84
in areas of mechanical stress, provide support by adhering 2 cells together in disk shape with cadherins
desmosome
85
tight junction everything
forms when EC surf of 2 adj. plasma membranes join together so not EC space remains between them - adhering junctions (desmosome) must form 1st - occurs in band around circumference of cell - joined at apical surf - limits movement thru EC space - limits paracellular diffusion - forces passage thru cells and NOT between (NO LEAKS) - Claudin composition - prevent epithelial mesenchymal transition - encircle epithelial cell by connecting to actin microfilaments - ZO-1 acts to tether cytoskeleton to transmembrane barrier protein
86
occurs in band around circumference of cell after an adherins/desmosome leaving so EC space between the cells
tight junctions of epithelial cells - at apical surf
87
composition includes claudin
TJ
88
limits movement through EC space, limits paracellular diffusion, prevents Epithelial mesenchymal transition
TJ force passage thru cells and not leaking between
89
connect to actin MFs
TJs
90
gap junction
protein channels linking cytosol of adjacent cells - connexins proteins small diam. of channel limits passage thru to small ions
91
protein channels linking cytosol of adjacent cells
gap junction
92
nucleus
Nuclear envelope contains 2 membranes with nuclear pores. RNA moves thru pores. DNA forms w histones into chromatin (dense) chromatin becomes chromosomes
93
free ribosomes
release proteins into cytosol
94
rough ER
proteins synthesized here pass into lumen of ER and then Golgi and secreted out
95
smooth ER
lipid molecules synthesized. stores Ca2+ for muscle contractions
96
golgi
prots arrive from rough er and undergo mods and sorting with transport vesicles
97
mitochondria organelle
chem process transfer energy from bonds to ATP most ATP formed in mitochondria BY CELLULAR RESPIRATION - inner and outer membrane - inner membrane folded has crustal into the matrix
98
cellular respiration
produces most ATP in mitochondria consumes O2 and produces, CO2, heat water
99
mitochondria membranes
inner and outer inner folds into crustal, extends into matrix
100
lysosomes
have acidic fluid w digestive enzymes defense break down
101
peroxisomes
consume molecular oxygen NOT used in transfer of energy to ATP removes H from organic molecules prods H2O2 toxic in high conc. break down fatty acids in 2C sources which can be used for ATP
102
cytoskeleton
formed by protein filaments determines cell shape, movements and contractions - actin filaments = microfilaments (thin) - IM - microtubules (tubulin units)
103
IM filaments
assoc w desmosomes to provide support/stability
104
microtubules
hollow tubulin protein subunits rigid, in neurons radiate from centrosome cilia core
105
cilia
core of microtubules motile on epithelial cells (move mucus)
106
no signal sequence
synthesis continues on free ribosome and then released into cytosol, destined for function in cell/enzyme
107
proteome
the specific proteins expressed in a cell
108
protein degradation
some have high affinity for proteolytic enzymes unfolded plots more easily digested targeted for degradation by attachment of ubiquitin which directs the protein to a proteasome
109
proteasome
protein complex that unfolds and breaks down a protein
110
ubiquitin
regulatory protein that targets proteins for degradation by proteasome - covalent attachment to lysine
111
specificity
depends on shape of binding site ability of protein to bind active site
112
affinity
strength of ligand-protein binding depends on strength and attraction between protein-ligand with high affinity, very little ligand is required to bind
113
saturation
fraction of total binding sites that are occupied % saturation depends on [unbound ligand] and affinity of binding site for the ligand - if binding site had high affinity, low [ligand] conc. will result in high saturation bc once bound to site, ligand not easily dislodged
114
competition
the ability and presence of 1+ ligands to bind to same binding site affects the % of occupation - cooperation
115
allosteric modulation
as shape of binding site changes, cooperation changes shape of other regions of the protein non covalent binding of ligand to 1 site can alter the shape and binding characteristics (affinity) active site for binding and regulatory binding site modulators bind regulatory site
116
Hb EX
4 subunits for O2. when 1 O binds, affinity of other sites for O2 increase
117
covalent mods
often phosphate group (-) added charge alters distribution of electrical forces and changes conformation protein kinase mediates phosphorylation
118
kinase
proteins modulates phosphorylation catalyze transfer of Pi from ATP to OH on side chain
119
phosphatase
dephosphorylation
120
metabolism
cells cannot use heat energy synthesis and breakdown of organic molecules req'd for structure and function generates water
121
reaction rate is influenced by
reactant conc. activation energy temperature catalysts
122
active site
region of enzyme that binds substrate
123
cofactors
trace metals bind and work with the enzyme can alter enzyme conformation
124
coenzyme
cofactor that directly participates as a substrate in a reaction. the coenzyme remains in original form throughout derived from vitamins, NAD+, FAD
125
oxidized
lose electrons
126
loss of electrons
oxidation
127
gain electron
reduced
128
reduced
gain electrons
129
ATP
primary molecule that stores energy transferred from breakdown
130
glycolysis
carbs (glucose) only sugar breakdown/catalysis 10 enzymatic reactions NO Oxygen Occur in cytosol break down 6C glucose into 2 3C pyruvate (ionized pyruvic acid) Net GAIN of 2 ATP, 4 H (2 released), 2 transferred NAD+ All IMs between glucose and pyruvate end prod contain ionized phosphate groups (remain trapped in cells since cannot penetrate plasma membrane) most pyruvate is reduced to lactate
131
where is glycolysis
in cytoplasm, NO oxygen
132
1st step of (an)aerobic respiration
glycolysis in cytoplasm
133
glycolysis process
glucose broken down into 2 3C pyruvates. then, either lactate or to krebs cycle
134
pyruvate
2 3C pyruvate formed by glycolysis mostly reduced to lactate otherwise onto kreb's cycle
135
pyruvate reduced to lactate
2 3C pyruvate of glycolysis reduced to lactate 1. 2 H atoms from NADH+ and H+ transferred to pyruvates molecules to form lactate and NAD+ is regenerated 2. remainder of pyruvate is not converted to lactate but enters kreb's to be broken down to CO2 lactate released into blood, liver (precursor to glucose) converted back into pyruvate, used as energy source
136
Kreb's cycle
citric acid cycle forms CO2, some ATP in the inner mitochondrial matrix pyruvate enters mitochondria from cytosol metabolized into 2C acetyl coA (release CO2) 1. primary molecule: acetyl coenzyme A coA transfers acetyl group to 4C oxaloacetate to form 6C citrate - acetyl-CoA reacts --> generation of reduced cofactors NADH and FADH2, production of ATP thru substrate-level phosphorylation. directly prods 1 high E NTP
137
Krebs cycle conditions
ONLY AEROBIC oxidative phosphorylation is necessary for regeneration of H-free form of coenzymes used in oxidative phosphorylation to form lots of ATP
138
reduced cofactors
NADH, FADH2
139
oxidative phosphorylation
most important mechanism for energy derivation energy for ATP derived from energy - mitochondria - aerobic E released when H ions combine with molecular O2 to form H2O H comes from NADH, H+, FADH2 coenzymes of Kreb's cycle, by metabolism of fatty acids -embedded in mitochondrial membrane is ATP synthase - forms channels
140
coenzymes of krebs cycle
soluble in mitochondrial matrix
141
cytochromes
proteins contain iron heme and copper cofactors form components of electron transport chain and transfer electrons: - 2 e- from H are transferred ... eventually to O2 to form water
142
potential energy of oxidative phosphorylation
hydrogen ion conc. gradient energy of gradient converted into chemical bond by ATP synthase (catalyzes formation of ATP from ADP)
143
ATP synthase
embedded in mitochondrial membrane forms channels
144
step forming the most ATP
oxidative phosphorylation in inner mitochondrial membrane, aerobic
145
occurs at inner mitochondrial membrane
krebs (cofactors) and oxidative phosphorylation (most ATP)
146
glycogen storage
muscles and liver synthesis from glucose
147
synthesis of glycogen
add phosphate group to glucose, form glucose 6 phosphate to be broken down to pyruvate to to form glycogen
148
gluconeogenesis
major substrate is pyruvate formed from lactate liver and kidneys
149
essential amino acids
9/20
150
vitamins
diff solubility water soluble vitamins form parts of coenzymes like NAD+, FAD+, coA
151
hypoxia
lack of O2
152
Tylenol case study
cause of death was hypoxia (low O2) despite blood oxygen levels elevated cell death and mitochondrial damage BC oxygen not delivered to tissues, accumulated in blood O is final electron acceptor
153
stripping electrons
carbons become more oxidized for ETC
154
NAD+
oxidized acceptor
155
NADH
reduced donor
156
reduced
has the H
157
why are ppl so vulnerable to protein deficiency
no essential amino acids can be synthesized by the body, must be consumed
158
required for binding
concentration, orientation, and affinity binding is random
159
cytochrome C oxidase
enzyme; complex 4 of ETC transfers electrons to molecular O2 (substrate), reducing it to water
160
higher respiration
more water produced
161
law of mass action
drive rxn forward by increasing substrate. increase prods = drive backwards
162
when available ATP is exhausted
catabolism ensues
163
Km
measure of affinity strength/tightness of ligand-protein binding
164
simple diffusion
no energy input besides movement from heat, NO ATP; passive
165
graded potentials
magnitude is related to intensity of stimulus that elicits them
166
magnitude is related to intensity of stimulus that elicits them
graded potential
167
neuronal time constant
proportional to product of membrane resistance and capacitance
168
proportional to product of membrane resistance and capacitance
neuronal time constant
169
speed of conduction of nerve impulse can be determined by
temperature and diameter of axon
170
If apply Na channel agonist to squid axon that is voltage clamped to -100mV...
large inward sodium current AND voltage gated K+ channels remain closed
171
EX of synaptic plasticity
1. increasing amount of NT released from AP 2. Increasing number of receptors on postsynaptic membrane 3. altering amount of Ca entering the cell at presynaptic terminus
172
stimulus intensity/strength is encoded in
freq. of Pas with stronger stimuli eliciting higher frequencies
173
Serotonin
excitatory NT
174
Effect of fluoxetine in post-synaptic neuron
acts on serotonin - excitatory NT = graded potentials of longer duration in post-synaptic neuron
175
oxidative phosphorylation
1. ETC 2. chemiosmosis ATP synthase complex uses E released from ETC proton gradient to make ATP
176
electron transport chain
proteins bound to inner mitochondrial membrane; electrons pass through series of redox reactions, release energy transfers e- from reduced molecules onto O2 to become H2O (most reduced) as e- passed, E released and used to pump protons, create proton gradient (PE)
177
cellular respiration
1. glycolysis in cytosol AEROBIC, Mitochondria 2. krebs 3. oxidative phosphorylation & ETC
178
net products of glycolysis
2 ATP (net), 2 H+, 2 H2O, 2 NADH, 2 pyruvate (--> lactate)
179
glycolysis reaction
glucose + 2 ATP + 2 NAD+ --> 2 pyruvate, 4 ATP, 2 NADH, 2 H+, 2 H2O
180
all IMs contain ionized phosphate group so cant permeate membrane and leave
glycolysis in cytosol - body pH
181
step 4 glycolysis
fructose 1,6 - diphosphate splits into 2 molecules. isomerase converts 1 into the other so 2 of same molecule UNSTABLE bc 2 phosphate groups
182
step 1 glycolysis
glucose phosphorylated by kinase USE 1 ATP Mg2+ cofactor lowers Ea
183
step 2 glycolysis
becomes fructose
184
step 3 glycolysis
USE 2nd ATP w/ cofactor Mg to phosphorylate
185
step 5
split apart into 2. DHAP converts by isomerase into glyceraldehyde
186
step 6 glycolysis
2 NADH is reduced to 2 NAD+ and 2 H+ exergonic rxn releases energy to be used to phosphorylate again
187
step 7 glycolysis
ATP Is formed x2 from each molecule SUBSTRATE LEVEL PHOSPHORYLATION: Pi transferred from IM substrate onto an ADP
188
glycolysis step 8/9
isomerize and LOOSE WATER = PEP is unstable and looses phosphate group x2
189
step 10 glycolysis
unstable PEP x2 donates it phosphate group to ADP = 2 ATP and becomes 2 pyruvate (end prod) - go on to krebs and make CO2 or - into lactate
190
end of glycolysis
if oxygen is available, krebs and ETC breaks down pyruvate all the way into ATP
191
what does glycolysis NEED
2 ATP energy carbohydrate 2 NAD+
192
NADH/NAD+ cycling
Oxygen: NADH can pass its electrons into the electron transport chain, regenerating NAD+ glycolysis. Anaerobic: fermentation
193
erythrocytes
RBCs have enzymes for glycolysis but NO MITOCHONDRIA so no other pathways
194
lactate
prod during muscle activity released into blood - can be converted back into pyruvate (oxidized) - used as precursor in liver to form glucose
195
use of lactate
released into bloodstream - converted back into pyruvate - or stored in liver as precursor to glucose
196
critic acid cycle facts
uses carbs, fats, and proteins to prod CO2, H atoms (half bound to coenzymes), some ATP
197
step 1 krebs
1. Acetyl coA forms citrate (transfer acetyl group from coA onto oxaloacetate) pyruvate enters mitochondria from cytosol after glycolysis metabolized into acetyl coA and CO2 NAD+ --> NADH
198
acetyl coA
enzyme derived from vitamin B transfer acetyl group w/ pyruvate or fatty acid breakdown 1st step of krebs produced from OXIDATION OF PYRUVATE
199
krebs step 2
citrate isomerized with loss/addition of water molecule
200
krebs step 3
isocitrate is oxidized and releases CO2 NAD+ is reduced to NADH
201
krebs production of ATP
directly prods 1 high E GTP --> ATP uses substrate level phosphorylation
202
How kreb's creates ATP
substrate level phosphorylation: Pi onto GDP = GTP GTP + ADP = ATP + GDP creates ATP from GTP
203
Krebs cycle most important
H atoms transferred to reduce coenzymes and free H generated are used in oxidative phosphorylation to gen. ATP
204
reaction of krebs
Acetyl CoA + 3 NAD+ + FAD + GDP + Pi + 2 H2O --> 2 CO2, CoA, 3 NADH, 3H+, FADH2, GTP
205
why must oxidative phosphorylation/krebs be aerobic
nec. for regeneration of oxidized, H-free form of coenzymes mitochondria CANNOT remove H from coenzymes under anaerobic conds
206
step 4 krebs
reduced NAD+ to NADH release CO2 forms succinyl coA
207
step 5 krebs
CoA group of succinylcholine CoA is replaced by phosphate, then transferred to ADP to make ATP = succinate
208
step 6 krebs
succinate oxidized. 2 H atoms are transferred to FAD = FADH2
209
7/8 krebs
water added, converts molecule and malate regenerates into starting oxaloacetate NAD+ is reduced to NADH
210
products of citric acid cycle
2 C enter on acetyl CoA 2 CO2 released 3 NADH 1 FADH2 1 ATP per acetyl coA
211
why krebs cant operate without O2
when ET cant oxidize NADH to NAD+, there is no NAD+ available for krebs (finite)
212
krebs regulation
by oxygen and availability of NAD+
213
oxidative phosphorylation ENERGY
E transferred to ATP is derived from E released when H ions combine w/ molecular O2 to form H2O H comes from NADH + H+ and FADH2 coenzymes generated in krebs (metabolism of fatty acids (and glycolysis)) as e= are transferred from 1 protein to another, some E released is used by cytochromes to PUMP H ions from matrix to intermemb. space = CREATES SOURCE OF PE AS H+ ION CONC. GRADIENT
214
oxidative phosphorylation EQ
1/2 O2 + NADH + H+ --> H2O + NAD + E
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Krebs cycle enzymes
soluble in mitochondrial matrix
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proteins of oxiphospho
embedded in mitochondrial membrane 1. transfer H onto molecular O2 2. couple E released to synthesis of ATP
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ETC components
cytochromes (Fe and Cu cofactors) transfer H down to O2 with proteins
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general ETC
2 H e- are transferred from NADH + H+ or FADH thru the chain w/ cofactor until reach O2 and form H2O - use free H ions and coenzyme H ions
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oxidized H-free coenzymes
regenerated in ETC so available to accept 2 more H from other paths ETC regenerates H-free oxidized coenzymes NAD+ and FAD by transferring the H onto O2 rxns prod. conc gradient flow of H+ back across membrane provides E for ATP synthase
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coenzymes of krebs
oxidized in ETC so now available to accept 2 more H
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H ion conc gradient
PE source of ETC e- are transferred from 1 protein to another, releasing E to be used by cytochromes to pump the ions from the matrix into intermembrane space
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ATP synthase
embedded in mitochondrial membrane enzyme that forms a channel in membrane allowing H ions to flow to matrix side
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reason for channel/conc gradient in ETC
lipid bilayer blocks diffusion of ions ATP synthase creates channel for H ions to flow to matrix side = chemiosmosis
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conc gradient of ETC Energy
E converted to chemical BOND E by ATP synthase, catalyzes form of ATP from ADP
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chemiosmosis
ATP synthase embedded in mitochondrial membrane that forms channel in membrane allowing H ions to flow to matrix side
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most ATP is formed
oxidaphosphorylation from H atoms of Krebs cycle (breakdown macromolecules)
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mitochondria
prods most ATP, consumes most O2, releases most CO2
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entering substrate of ETC
H atoms of NADH + H+ and FADH2; O2 formed during glycolysis and krebs
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products of ETC
2-3 ATP for each NADH + H+ 1-2 ATP for each FADH2
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carb catabolism
breakdown carb to pyruvate or lactate by glycolysis metabolize pyruvate to CO2 and H2O by krebs and ox phosphorylation
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substrate level phosphorylation
glycolysis and krebs net gain of 2 ATP from glycolysis 2 more ATP from krebs GTP - 1 ATP for each of 2 pyruvate molecules entering cycle
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max ATP
34 ATP
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ATP production of krebs
glucose --> 2 pyruvate molecules --> 2 GTP --> 2 ATP (substrate level phosphorylation)
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Anaerobic ATP production
only 2 ATP from substrate level phosphorylation in glycolysis -> lactate
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energy in Anaerobic conditions
2 ATP from glycolysis lots of glucose break down into lactate
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glycogen
small amounts of glucose can be stored as reserve as polysaccharide glycogen, in liver and muscles
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glycogen synthesis
from glucose enzymes in cytosol 1. transfer phosphate from ATP to glucose SAME 1st step as glycolysis So, IM can be broken down to pyruvate or glycogen
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glucose storage
as glycogen in liver/muscles (polysaccharides)
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glycogen synthesis pathways
1. catabolized to provide energy for ATP formation 2. in liver cells, converted to free glucose by removal of phosphate group, then glucose can enter blood
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glucose synthesis
1. in liver, breakdown glycogen gluconeogenesis
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gluconeogenesis
generate new glucose from noncarbohydrate precursors major substrate is pyruvate, formed from lactate
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what determines if glucose is broken down to pyruvate or if pyruvate is used to synthesize glucose?
concentrations of glucose and pyruvate and hormones that alter/change expression
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adipocyte function
synthesize and store triglycerides, release as needed for E and ATP formation
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beta oxidation
coA derivative of fatty acid goes thru process which splits off acetyl coA and transfer 2 pairs of H atoms to enzymes ( 1 to FAD and 1 to NAD+) H atoms from co enzymes then enter oxidative phosphorylation path to form ATP
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ATP formed from fatty acid catabolism
18 C saturated = 146 ATP 1 glucose yields max 38 ATP catabolism of 1g fat is 2.5x greater than 1g carb
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fatty acid synthesis
1. cytoplasmic acetyl coA transfers acetyl group to another and start forming chain, repetition builds up by 2C at a time all fatty acids synthesized have even #
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acetyl coA enzyme
starting material for fatty acid synthesis, Krebs cycle, formed from pyruvate
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acetal coA derived from fatty acid breakdown
CANNOT be used to synth new glucose 1. pyruvate broken down into acetyl coA and CO2 is irreversible 2. the 2 C atoms in acetyl coA are used to form 2 molecules of CO2 during krebs
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glucose and fatty acids
glucose can readily be metabolized to synthesize fat fatty acids can NOT be used to synth glucose
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proteases
protein catabolism break peptide bonds
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macromolecules
all can enter the Krebs cycle thru some IM all can be used as source of E for synthesis of ATP
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keto acids
formed by removal of amino groups from AAs
253
ammonia
used to form urea in liver; excreted in urine
254
essential nutrients
water (body looses more than oxphospho prods) HILK MF TVW
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water soluble vitamins
form coenzymes NAD+, FAD, coA excreted in urine - accumulation in body is limited
256
fat soluble vitamins
ADEK are not coenzymes A - retinol
257
what structure contains enzyme required for oxidative phosphorylation
inner membrane of mitochondria NOT matrix
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ligand-protein binding reaction
allosteric modulation can alter affinity of protein for ligand phosphorylation of protein is a covalent mod if 2 ligands can bind same binding site of protein, = competition binding reactions are electrical or hydrophobic
259
what can be used to synthesize glucose by glujconeogeneis in liver?
glycerol (?)
260
catabolism of fatty acids
2 steps
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strength of ligand protein binding of binding site is
affinity
262
membrane structures that form channel linking together the cytosol of 2 cells and permitting movements of substances between cells
gap junction
263
fluid inside cells but NOT within organelles
cytosol liquid portion of the cytoplasm, excluding the organelles
264
significance of folds on inner mitochondrial membrane
increases total SA enzymes required to generate ATP are here structure --> function
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proteins and ligands relationship
protein function can be altered by allosteric changes in structure charge attraction
266
energy for homeostasis
ATP provides E required for homeostatic processes generation of ATP is under NEGATIVE feedback control.