Test 4 Flashcards

Question

Hydrogenation

Answer 1

- Addition of a hydrogen across double bond increases the degree of saturation - Many food products are produced by partial hydrogenation of oils and fats peanut oil+H2=Peanut butter

Answer 2

- hydrolysis - in the body - saponification - making soap - hydrogenation - adding H2 to increase saturation - --partial hydrogenation - semi-solids, examples: pb, margarine, shortening - oxidation - breaks the carbon-carbon bonds and forms smaller molecules. Causes fats and oils to go rancid - --antioxidants added to food to prevent oxidation (vitamin E and C and BHT,BHA (synthetic))

Answer 3

Hydrolysis in a basic solution -produce salt of fatty acid and glycerol solid soap = when NaOH used liquid soap = when KOH used

Answer 4

Phospholipid

Answer 5

Contains 2 fatty acids and phosphate group esterified to a glycerol molecule and an alcohol esterified to the phosphate group

Answer 6

Hydrolysis and saponification

Answer 7

Function as components of cell membranes

Answer 8

One fatty acid, one phosphate group with an alcohol group attached to the phosphate group

Answer 9

sphingophospholipids in which the alcohol esterified to the phosphate group is choline -found in all cell membranes and are important structural components of the myelin sheath of neurons

Answer 10

Contains both a fatty acid and a carbohydrate component

Answer 11

Simple sphingoglycolipids | -contain a single monosaccharide unit either glucose or galactose

Answer 12

Sphingomyelin

Answer 13

are complex sphingoglycolipids which can contain a branched chain of up to seven monosaccharide residue -found in the gray matter of the brain as well as in the myelin sheath

Answer 14

- membrane lipid - fused rings: 3, 6 carbon rings and one 5 carbon ring - important in human cell membranes, nerve tissue and brain tissue

Answer 15

- obtained from meats, milk, and eggs | - liver synthesized cholesterol

Answer 16

-carry cholesterol in the body, combination of lipids with proteins and phospholipids

Answer 17

low density - bad cholesterol - transports cholesterol to tissues where it can be used for synthesis of membranes and steroid hormones - deposit cholesterol in the arteries in the form of plaque when cholesterol intake exceeds what is needed by tissues

Answer 18

good cholesterol - more dense than LDL, more protein present - pick up cholesterol from the tissues and carry it to the liver, where it can be converted to bile salts, which are eliminated from the body

Answer 19

-blood test that measures serum lipid levels

Answer 20

Lipid based structure that separates the aqueous part of the cell interior from the exterior -lipid bilayer = two layer thick structure of phospholipids and glycolipids

Answer 21

- helps regulate membrane fluidity - fused ring system does not allow rotation of fatty acid tails in the vicinity - makes the membrane rigid (acts as a plasticizer)

Answer 22

Substances move across a cell membrane from a high to low concentration without using energy

Answer 23

Substances move across the cell membrane from a high to low concentration with the aid of membrane proteins with turing cell energy

Answer 24

Uses cell energy to pump membrane proteins to carry substances across the membrane from a low to high concentration

Answer 25

Disperses and stabilizes water-insoluble substances as colloidal participles in an aqueous solution

Answer 26

Cholesterol derivative that functions as an emulsifying agent, makes lipids soluble in the digestive tract, so they can be digested and absorbed

Answer 27

Fluid containing bile acid secreted from the liver and then stored in the gallbladder

Answer 28

- synthesized from cholesterol in the liver - stored in gall bladder and secreted into all intestine - have polar and non polar region - help in the absorption of cholesterol into the intestinal mucosa

Answer 29

- formed when large amounts of cholesterol accumulate in the gallbaldder - composed of almost 100% cholesterol, with some calcium salts, fatty acids, and glycerophospholipids

Answer 30

- messenger lipid - substances produced by a ductless gland - produced from cholesterol - include: sex hormones such as testosterone, and estrogen

Answer 31

Produced from the adrenal glands located on top of each kidney

Answer 32

- mineralocorticoid - control balance of Na+ and K+ ions | - glucocorticoids - control glucose metabolism and counteract inflammation

Answer 33

regulates electrolytes and water balance by the kidneys

Answer 34

Released under stress to increase blood sugar and regulate carbohydrate, fat and protein metabolism

Answer 35

Synthetic corticosteroid, derived from cortisone, used for reducing inflammation, treating asthma and rheumatoid arthritis

Answer 36

- oxygenated C20 fatty acid derivative that function as messengers - have profound effects at extremely low concentrations - hormone like - exert effects in the tissues where they are synthesized

Answer 37

- inflammatory response - production of pain and fever - regulation of blood pressure - induction of blood clotting - reproductive functions such as induction of labor - regulation of sleep/wake cycle

Answer 38

- prostaglandins - thromboxanes - leukotrienes

Answer 39

Regulates many functions in body - involved in raising body temp - inhibits secretion of gastric juices - increasing secreting of protective mucus layer into the stomach - relaxing and contracting smooth muscle, directing water/electrolyte balance, and enhancing inflammation response

Answer 40

Promote platelet aggregation (formation of blood clots)

Answer 41

Found in white blood cells, promote inflammatory and hypersensitivity responses

Answer 42

Block production of prostaglandins thus decreasing pain, inflammation and fever

Answer 43

Lipid with a monster of long chain fatty acid and a long chain alcohol

Answer 44

-water insoluble and water repellent

Answer 45

- protect hair, and skin and keep it pliable and lubricated | - impart water repellency to animal fur

Answer 46

Polymer of amino acids

Answer 47

Molecule containing both an amine, NH2 group and a carboxylic acid -amino acid are always alpha (α) amino acid because both the carboxyl group and amine group are attached to the alpha carbon

Answer 48

The only amino acid with a sulfhydryl group

Answer 49

1 amine group & 1 carboxyl group with nonpolar side chain

Answer 50

1 amine group & 1 carboxyl group with polar side chain, but neutral

Answer 51

1 amine group & 2carboxyl groups with side chain containing 2nd –COOH group

Answer 52

2 amine groups & 1 carboxyl group with side chain containing 2nd amine group

Answer 53

needed by the human body, but must come from dietary sources

Answer 54

NH2 on the left

Answer 55

NH2 on the right

Answer 56

Chain of covalently linked amino acids | -covalent bonds between amino acids in a peptide are called peptide bonds

Answer 57

bond between two amino acids

Answer 58

bond between ~ 10 - 20 amino acid

Answer 59

bond between large number of amino acids

Answer 60

``` Three letter abbreviations - widely used for naming: First letter of amino acid name is compulsory and capitalized followed by next two letters not capitalized except in the case of Asparagine (Asn), Glutamine (Gln) and tryptophan (Trp) ```

Answer 61

Peptides that contain the same amino acids but present in different order are different molecules (constitutional isomers) with different properties

Answer 62

Many relatively small peptides are biochemically active: - Hormones - Neurotransmitters - Antioxidants

Answer 63

Small peptide neurotransmitters - are pentapeptide neurotransmitters produced by the brain and bind receptor within the brain - help reduce pain

Answer 64

1. splits the peptide bonds to give smaller peptides and amino acids. 2. occurs in the digestion of proteins. 3. occurs in cells when amino acids are needed to synthesize new proteins and repair tissues.

Answer 65

1. In the lab, the hydrolysis of a peptide requires acid or base, water, and heat. 2. In the body, enzymes catalyze the hydrolysis of proteins.

Answer 66

- small peptide antioxidants - present in high levels in most cells - regulator of oxidation/reduction reactions - antioxidant

Answer 67

A naturally-occurring, unbranched polymer, peptide in which at least 40 amino acid residues are present - Monomeric protein contains one peptide chain - Multimeric protein contains more than one peptide chain

Answer 68

A protein in which only amino acid residues are present

Answer 69

A protein that has one or more non-amino acid group present in its structure -(non-amino acid components) may be organic or inorganic

Answer 70

refers to the order in which amino acids are linked together in a protein -Insulin was the 1st to have its order of amino acids determined (51 A.A.) -Frederick Sanger (1953) sequenced and determined the primary structure for the first protein - Insulin

Answer 71

arrangement in space (backbone portion of protein) | -alpha helix, or beta pleated sheet

Answer 72

overall 3-dimensional shape of a protein that results from the interactions between amino acid side chains (R-groups) that are widely separated from each other with in peptide chains

Answer 73

1. Covalent disulfide bonds (strongest) 2. Electrostatic attractions or salt bridges (acidic side chain & basic side chain) 3. Hydrogen bonds (between amino acids with polar R group) 4. Hydrophobic attractions (2 nonpolar side chain)

Answer 74

organization among various polypeptides in multi chain protein 1. Electrostatic interaction 2. Hydrogen bonds 3. Hydrophobic interaction 4. the combination of two or more polypeptide chains. 5. stabilized by the same interactions found in tertiary structures. 6. of hemoglobin consists of two alpha chains and two beta chains with heme groups in each subunit that pick up oxygen for transport in the blood to the tissues.

Answer 75

1. membrane 2. fibrous 3. globular

Answer 76

associated with cell membranes - insoluble in water - help in transport molecule across the membrane

Answer 77

polypeptide chains arranged in long strands or sheets (insoluble) 1. keratins - found in wool, feathers, hooves, silk, hair and fingernails 2. Collagens - found in tendons, bone and other connective tissue 3. Elastins - found in blood vessels and ligaments 4. Myosin – found in muscle fissure 5. Fibrin – found in blood clots

Answer 78

polypeptide chains are folded into spherical or globular proteins (soluble) 1. Insulin – regulatory hormone for controlling glucose metabolism 2. Myoglobin – involved in oxygen transport in muscles 3. Hemoglobin – involved in oxygen transport in blood 4. Transferring – involved in iron transport in blood 5. Immunogloblin – involved in immune system responses

Answer 79

-30% of body ( must abundant protein) found in tendons, ligaments, blood vessels and skin made up of triple helices which cross-link cross-linking gives more strength (more rigid) {causes aging}

Answer 80

transports oxygen from lungs

Answer 81

oxygen storage in the muscles

Answer 82

1. Catalytic 2. Defense 3. Transport 4. Messenger 5. Contractile 6. Structural 7. Transmembrane 8. Storage 9. Regulatory 10. Nutrient

Answer 83

Enzymes are best known for their catalytic role.

Answer 84

Immunoglobulins or antibodies are central to functioning of the body’s immune system

Answer 85

Bind small biomolecules, e.g., oxygen and other ligands, and transport them to other locations in the body and release them on demand.

Answer 86

transmit signals to coordinate biochemical processes between different cells, tissues, and organs.

Answer 87

Necessary for all forms of movement.

Answer 88

Confer stiffness and rigidity

Answer 89

Span a cell membrane and help control the movement of small molecules and ions.

Answer 90

Bind (and store) small molecules.

Answer 91

Often found “embedded” in the exterior surface of cell membranes - act as sites for receptor molecules

Answer 92

Particularly important in the early stages of life - from embryo to infant.

Answer 93

1. the disruption of bonds in the secondary, tertiary, and quaternary protein structures. 2. heat and organic compounds that break apart H bonds and disrupt hydrophobic interactions. 3. acids and bases that break H bonds between polar R groups and disrupt ionic bonds. 4. heavy metal ions that react with S—S bonds to form solids. 5. agitation, such as whipping, that stretches peptide chains until bonds break

Answer 94

-partial or complete disorganization of a protein’s tertiary structure -Microorganisms are killed by denaturation of proteins -Fever over 104ºF will start to denature the critical enzymes of the body -

Answer 95

Precipitation (denaturation of proteins) Egg white - a concentrated solution of protein albumin

Answer 96

protein that contains carbohydrates in addition to amino acid -collagen (when heated with strong base produces water soluble protein gelatin)

Answer 97

a conjugated protein that contains lipids in addition to amino acids

Answer 98

glycoprotein molecule produced by an organism as a protective response to the invasion of microorganisms or foreign molecule

Answer 99

foreign substance in the body bacterium or virus

Answer 100

biochemical molecule that counteracts specific antigens

Answer 101

Proteins that catalyze nearly all the chemical reactions taking place in the cells of the body -increases the rate of reactions by lowering the energy of activation -most enzymes are globular proteins -enzymes under go all the reactions of proteins – including denaturation -are most active at an optimum temperature (usually 37 C in humans) -show little activity at low temperatures lose activity at high temperatures as denaturation occurs

Answer 102

Contains an enzyme used to speed up the decomposition of glucose to produce CO2 and ethanol in bread, wine, etc.

Answer 103

enzymes made of ribonucleic acid instead of protein

Answer 104

Enzyme composed only of protein (amino acid chains)

Answer 105

Enzyme that has non-protein and | protein parts

Answer 106

Protein part of a conjugated enzyme

Answer 107

Non-protein part of a conjugated enzyme (derived from dietary vitamins)

Answer 108

Biochemically active conjugated enzyme | Apoenzyme + cofactor = holoenzyme

Answer 109

Suffix -ase identifies an enzyme | -some of the digestive enzymes have -in at the end (pepsin, trypsin and chymotrypsin)

Answer 110

1. oxidoreductase - oxidation reduction 2. Transferase - transfer of functional group from one molecule to another 3. Hydrolase - addition of water molecule 4. Lyase - addition or removal of a group to a double bond 5. Isomerase - rearrangement of functional group within a molecule 6. ligase - bonding together two molecules into one

Answer 111

Oxidation and reduction reactions are always linked to one another -Lactate dehydrogenase is an oxidoreductase

Answer 112

Two major subtypes: - Transaminases - catalyze transfer of an amino group to a substrate - Kinases - catalyze transfer of a phosphate group from adenosine triphosphate (ATP) to a substrate

Answer 113

- Involves addition of a water molecule to a bond to cause bond breakage - Hydrolysis reactions are central to the process of digestion: - -Carbohydrases hydrolyze glycosidic bonds in oligo- and polysaccharides - -Proteases effect the breaking of peptide linkages in proteins - -Lipases effect the breaking of ester linkages in triacylglycerols

Answer 114

- Dehydratase: effects the removal of the components of water from a double bond - Hydratase: effects the addition of the components of water to a double bonds

Answer 115

Is an enzyme that catalyzes the isomerization (rearrangement of atoms) reactions.

Answer 116

Is an enzyme that catalyzes the formation of a bond between two molecules involving ATP hydrolysis: - ATP hydrolysis is required because such reactions are energetically unfavorable - Require the simultaneous input of energy obtained by a hydrolysis of ATP to ADP

Answer 117

reactant in an enzyme-catalyzed reaction (substance upon the enzyme “acts")

Answer 118

The small part of the enzyme structure where the reaction occurs -Formed due to folding and bending of the protein -Usually a crevice like location in the enzyme

Answer 119

Small part of an enzyme’s structure that is involved in catalysis

Answer 120

intermediate reaction site formed when the substrate binds to the active site of the enzyme

Answer 121

fixed, rigid geometrical conformation Only substrates with a complementary geometry can be accommodated at the site

Answer 122

flexible active site that adapt to the substrate

Answer 123

the limitation of an enzyme to catalyze one specific reaction with one specific substrate

Answer 124

(enzyme – urease catalyzes only the hydrolysis of urea, but no other amides)

Answer 125

(glucose oxidase oxidizes only D-glucose not L-glucose)

Answer 126

(act only on molecules that have a specific functional group)

Answer 127

(Enzyme will act on a particular type of chemical bond, rest of the molecular structure is not considered)

Answer 128

- optimum temperature - optimum pH - substrate concentration - enzyme concentration

Answer 129

An increase in substrate concentration: -increases the rate of reaction (at constant enzyme concentration) -eventually saturates an enzyme with substrate to give maximum activity. Limit of substrate saturation -Substrate concentration reaches its maximum rate -All the active sites are full

Answer 130

Number of substrate molecules converted to product per minute by one molecule of enzyme under optimum conditions of temperature, pH, and saturation

Answer 131

-Organisms that thrive in extreme environments -Microbial enzymes that are active at conditions that would inactivate human enzymes and enzymes present in other higher organisms

Answer 132

substance that slow or stops an enzyme reaction by binding to it

Answer 133

has a chemical structure and polarity that is similar to that of the substrate. competes with the substrate for the active site. has its effect reversed by increasing substrate concentration

Answer 134

-decreases enzyme activity by binding to a site on an enzyme other than the active site Causes a change in the structure of the enzyme Prevents the catalytic groups at the active site from properly effecting their catalyzing action Increasing the concentration of substrate does not completely overcome inhibition

Answer 135

Inactivates enzymes by forming a strong covalent bond to an amino acid side-chain group with the enzyme’s active site Does not have a structure similar to that of the enzyme’s normal substrate Increasing substrate concentration does not reverse the inhibition process Enzyme is permanently inactivated

Answer 136

substance that kill bacteria or inhibits their growth

Answer 137

antibiotic – (first one – sulfanilamide) It inhibits bacterial growth because it is similar to PABA (p-aminobenzoic acid). Many bacteria need PABA as a coenzyme

Answer 138

most widely used antibiotic (It weakens the cell walls of bacteria)

Answer 139

ciprofloxacin hydrochloride – a broad spectrum antibiotic contains several common functional groups (carboxylic acid, ketone & amine)

Answer 140

- competitive inhibitors | - used to treat some infections

Answer 141

Catalyzes the breaking of peptide bonds

Answer 142

An inactive precursor of a proteolytic enzyme.

Answer 143

-Have quaternary structure --Composed of two or more protein subunits -Have at least two kinds of binding sites --Substrate and regulator binding sites Active and regulatory binding sites are distinct from each other in both location and shape

Answer 144

common clinical lab procedure – high urea levels in the blood indicate kidney malfunction

Answer 145

is an octapeptide hormone that increases blood pressure via constriction of blood vessels.

Answer 146

Converts Angiotensin I to angiotensin II in the blood -ACE inhibitors block ACE reaction and thus reduce blood pressure. Monoprilis an example of a ACE inhibitor

Answer 147

- Essential in some amounts for the proper functioning of the human body - Must come from dietary sources because the body cannot synthesize them - Conjugated enzymes contain vitamins as part of their structures

Answer 148

-Required in collagen -synthesis and healing of wounds -Found in blueberries, citrus fruits, strawberries, tomatoes Deficiencies are scurvy, weakened connective tissue, slow-healing wounds, and anemia

Answer 149

Found in liver, yeasts, whole grain bread | -Deficiencies lead to Beriberi

Answer 150

Found in liver, yeasts, nuts, eggs Deficiencies include dermatitis, loss of hair, fatigue, and anemia

Answer 151

Found in beef, liver, chicken, eggs, dairy foods Deficiencies lead to Dermatitis

Answer 152

- Found in chicken, beef, fish | - Deficiency can result in dermatitis, muscle fatigue, and loss of appetite

Answer 153

-Found in salmon, beef, liver, eggs, fresh vegetables -Deficiency can result in fatigue, retarded growth, cramps, and anemia

Answer 154

Found in liver, beef, kidney, fish, milk | -deficiencies are pernicious anemia, nerve damage, and malformed red blood cells

Answer 155

Deficiencies are abnormal red blood cells, anemia, and poor growth - The absence of folic acid increases the possibility of a neural tube defect (a defect in the development of the spinal cord). - Neural tube defects usually develop in the first 28 days of pregnancy, often before a woman even knows that she is pregnant.

Answer 156

Found in meat, liver, fish, nuts, spinach | -deficiency may lead to dermatitis, fatigue, and anemia

Answer 157

Major functions of A: 1. vision 2. regulating cell differentiation 3. maintenance of the health of epithelial tissues 4. reproduction and growth - deficiencies include night blindness, immune system repression, and slowed growth

Answer 158

``` is an antioxidant in cells is found in whole grains and vegetables has an RDA of 15 mg deficiencies are hemolysis and anemia 4 forms of vitamin E: 1. alpha 2. beta 3. delta 4. gamma-tocopherol ```

Answer 159

is essential to the blood-clotting process | -Deficiencies are prolonged bleeding time and bruising