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Human Nutrition > Protein and alcohol > Flashcards

Protein and alcohol Flashcards

1
Q

What macronutrients is comprised of a unique sequence patten of amino acids and contain nitrogen

A

protein

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2
Q

What proteins provides tissue support?

A

elastin
collagen

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3
Q

What proteins provide muscular structure and function?

A

myosin
actin
troponin
tropomyosin

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4
Q

What proteins transport substances throughout the body?

A

apoproteins
hemoglobin
albumin

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5
Q

What protein is responsible for blood clotting?

A

fibrin

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6
Q

what protein is responsible for blood thinning?

A

plasmin

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7
Q

How are proteins used for fluid balance?

A

when protein concentration in the blood are low, fluid “leaks” out of the blood into the interstitial space and causes swelling

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8
Q

What elements are amino acids composed of?

A

Carbon
Hydrogen
Oxygen
Nitrogen

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9
Q

What defines the protein in the molecular structure?

A

the unique side chain

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10
Q

what proteins contain sulfur in the side chains?

A

Cysteine and Methionine

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11
Q

Of the 140 AA found in nature, how many are used to make proteins?

A

20

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12
Q

What is the general molecule structure of AA?

A

a central Carbon
one carboxyl group (COOH)
at least one amine group (NH2)
a hydrogen atom
a unique side chain

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13
Q

How many essential amino acids must be consumed in the diet?

A

9

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14
Q

How many nonessential AA are there?

A

11

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15
Q

What type of bond is formed when the carbon of the acid group of one AA joins with the nitrogen atom of the amine group of a second AA

A

peptide bond

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16
Q

What reaction forms peptide bonds?

A

condensation

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17
Q

What reaction breaks peptide bonds?

A

hydrolysis

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18
Q

two AA joined together

A

dipeptide

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19
Q

3 AA joined together

A

tripeptide

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20
Q

4-9 AA joined together

A

oligopeptide

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21
Q

10+ AA joined together

A

polypeptide

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22
Q

The genetic information from DNA’s base sequence is copied to the base sequence in mRNA.

A

Transcription

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23
Q

single strand of nucleotides, with nitrogenous bases AGC, and U (uracil); also contains pentose sugar ribose instead of deoxyribose

A

RNA

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24
Q

the genetic information in RNA is converted into the AA sequence of a protein

A

Translation

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25
Q

What structure is the sequential order of the AA?

A

primary structure

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26
Q

What structure is the initial folding caused by interactions of the positively charged AA and negatively charged carboxylic acid groups?

A

secondary structure

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27
Q

What structure is the complex folding due to interactions among R-groups (with sulfur bonds being strongest)?

A

tertiary structure

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28
Q

what structure is two or more polypeptide chains bond together?

(not all proteins)

A

quaternary structure

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29
Q

What term describes the alteration of the protein’s shape (therefore, functions) through the use of heat, acids/bases, salts, mechanical agitation?

A

Denaturation of proteins

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30
Q

What structure of the protein is unchanged by denaturing?

A

primary structure

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31
Q

Where are proteins found in our diet?

A

animal meats, dairy products, and legumes
-excludes butter/sour cream/cream cheese

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32
Q

What digestion of protein occurs in the mouth?

A

none

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33
Q

What hormone stimulates the release of gastric juice?

A

gastrin

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34
Q

What does gastric juice contain that starts to denature proteins?

A

Hydrochloric acid (HCl)

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35
Q

What does the denaturing process from HCL do for digestive enzymes?

A

allows digestive enzymes access to the proteins

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36
Q

What bond is not affected by Hydrochloric acid (HCl) in the stomach?

A

peptide bonds

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37
Q

What enters the small intestine in the digestion process of proteins?

A

partially digested proteins
polypeptides

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38
Q

What stimulates the release of pancreatic juice?

A

cholecystokinin
CCK

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39
Q

What is pancreatic juice rich in?

A

proteases
inactive enzymes (zymogens or proenzymes)

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40
Q

within the small intestines, what are activated into functional proteases?

A

zymogens

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41
Q

What is located at the surface of the microvilli in the intestinal mucosal cells and yield individual AA (and some di and tripeptides)?

A

aminopeptidases

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42
Q

In the absorption process, What dictates the transporter used for AA?

A

features of the specific amino acid
-mass
-electrical charge
-side chain
etc.

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43
Q

in the absorption process, What do all AA transporters have in common?

A

carrier-mediated mechanism
energy in form of ATP is required

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44
Q

After absorption into the enterocyte, where do AA enter and travel too?

A

AA enter the portal circulation and travel to the liver, then other tissues

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45
Q

Do peptides absorb differently than AA?

A

yes

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46
Q

How do peptides absorb?

A

PEPT1 (for all di- and try-peptides)
once within enterocyte, peptides are hydrolyzed by cytosolic peptidases to generate free AA

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47
Q

What is the primary site for AA uptake following a protein-containing meal?

A

the liver

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48
Q

Do AA go through anabolic or catabolic processes in metabolization?

A

either anabolic or catabolic depending on the needs of the body

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49
Q

Anabolic or Catabolic?

Synthesis of a non-protein compound that contain nitrogen, including creatinine and serotonin

A

Anabolic

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50
Q

Anabolic or Catabolic?

Synthesis of body proteins, such as enzymes, antibodies, and various components of cells

A

anabolic

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51
Q

Anabolic or Catabolic?

synthesis of fat from amino acid carbon skeletons; this can be stored as adipose tissue

A

anabolic

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52
Q

Anabolic or Catabolic?

synthesis of glucose from amino acid carbon skeletons; this can be used for energy

A

catabolic

53
Q

Anabolic or Catabolic?

energy produced form amino acid carbon skeleton

A

catabolic

54
Q

What is a resource of all ‘free’ intra- and extracellular AA in the body?

A

Amino Acid pool

55
Q

How are AA in the pool used?

A

taken up by tissues and are used to meet the energy needs of various tissues

56
Q

How is the AA pool comprised?

A

arise from exogenous protein, degradation of endogenous protein, and synthesis of new amino acids

AA intermingle to form pool of about 150g

57
Q

What are the 3 anabolic fates of AA?

A
  1. building blocks for proteins
  2. building block for other nitrogen containing compounds
  3. conversion to fat for storage
58
Q

What hormone promotes protein synthesis?

A

insulin

59
Q

what stimulates protein synthesis?

A

periods of energy excess, but occurs continously because of the diverse functions

60
Q

what is:
-synthesized from glycine, cysteine and glutamate
-found in cytoplasm of cells in reduced (GSH) or oxidized form (GSSG)
-acts as an antioxidant

A

Glutathione

61
Q

the ratio of GSH:GSSG in cells is >10:1; a decrease in the GSH:GSSG is indicative of oxidatitive stress. Why?

A

The oxidized form (GSSG) increases

62
Q

What is:
-synthesized from lysine in the liver and kidneys and found in meat products
-needed for the transport of long chain fatty acids across the inner mitochondrial membrane for oxidation

A

carnitine

63
Q

what is:
- found in meat and fish and synthesized from arginine and glycine
- approx 95% in muscle, found in free and phosphorylated form
- replenish ATP during rapid contraction at the very onset of exercise
-damage to the heart causes enzyme to ‘leak’ out of heart; thus an elevated plasma level is used to diagnose a heart attack

A

creatine

64
Q

What is:
- synthesized from AA serine and found in eggs, meat, fish
- needed as a methyl donor, converts homocysteine to methionine; in the secretion of VLDL from the liver; and to form neurotransmitter acetylcholine
- deficient diets used in research to develop fatty liver in animals and may be associated with liver and heart disease in humans

A

choline

65
Q

What are the two main catabolic fates of AA?

A
  1. conversion to glucose for energy use
  2. oxidation of the carbon skeletons
66
Q

True or false:
proteins are being broken down and rebuilt continuously, irrespective of energy status

A

True

67
Q

What is the first step in AA catabolism and occurs by transamination and/or deamination?

A

removal of the amine group

68
Q

What process involves the transfer of an amino group from one AA to an a-keto acid (ie an AA carbon skeleton)

A

Transamination

69
Q

what catalyzes the AA in catabolism?

A

amino transferases aka transaminases

70
Q

what reaction involves only the removal of the amino group, with no transfer to another compound?

A

Deamination reaction

71
Q

What enzyme facilitates a deamination reaction?

A

deaminase/dehydratase enzymes

72
Q

what is produced from a deamination reaction?

A

a-keto acid and ammonium

73
Q

What is created from deamination reactions is very toxic and must be removed from the body?

A

ammonia

74
Q

what is the primary means of disposing ammonia?

A

urea cycle

75
Q

where does the urea cycle occur at?

A

in the liver and kidneys

76
Q

Where urea is formed, then transported to the kidneys, how is it excreted?

A

through the urine

77
Q

when urea created in the urea cycle travels in the blood from the liver to the kidney and is excreted, what can be measured and an indicator of renal health?

A

Blood Urea Nitrogen
BUN

78
Q

What BUN measurement can be signs of acute or chronic kidney dysfunction/failure?

A

> 20 mg/dL

79
Q

What two amino acids are completely ketogenic AA?

A

leucine and lysine because they do not make glucose

80
Q

from a metabolic standpoint, AA can be consider either:

A
  1. glucogenic
  2. ketogenic
81
Q

What type of AA are those that can be degraded to pyruvate, oxaloacetate, a-ketoglutarate, succinate, or fumarate and therefore can be converted into glucose through gluconeogenesis?

A

glucogenic AA

82
Q

what type of AA are those that can be converted into ketone bodies through ketogenesis?

A

ketogenic AA

83
Q

what is produced in the liver and transported to other tissues where they are reconverted to acetyl-CoA to produce energy via the TCA cycle and are used for fuel for the brain, heart, skeletal muscle, etc.

A

ketones

84
Q

What are the three essential branched chain AAs that are found in dairy and red meat, and often used to enhance performance, reduce muscle soreness, and faciliate muscle growth?

A
  1. isoleucine
  2. leucine
  3. valine
85
Q

what type of chain consists of a carbon atom bound to more than two other carbon atoms

A

side chain

86
Q

what enzymes are on skeletal muscle, heart, kidneys, and adipose tissue and can transaminate all three BCAA (branched chain amino acids)?

A

branched-chain aminotransferases

87
Q

What cycle describes:
- a removal of nitrogen from muscle (proteolysis)
- transfers the carbon structure of pyruvate liver where it can be converted to glucose
- synthesized glucose transports back to muscle and used for energy

A

Glucose alanine cycle

88
Q

How do we determine nitrogen balance?

A

N balance is calculated as the difference between nitrogen intake and nitrogen excretion.

2 week diet with specific nitrogen content given
amount of N collected in urine/feces

It’s easier to estimate (protein x 0.16)

89
Q

How are dietary proteins divided?

A
  1. complete (high quality)
  2. incomplete (low quality)
90
Q

What does the quality of protein depend on?

A
  1. digestibility
  2. its essential AA composition
91
Q

What protein category contains all the essential AA in the approximate amounts need?

A

complete protein

milk, yogurt, cheese, eggs, meat, fish, poultry

92
Q

What protein category has too little of one or more particular essential AA?

A

incomplete protein

legumes, vegetables, cereals, plan foods

93
Q

the essential AA that is present in the lowest quantity in the food

A

limiting AA

94
Q

What factors influence protein requirements?

A
  1. quality of protein
  2. body size
  3. physiologic state
  4. growth
  5. level of energy intake
  6. level/type of physical activity
95
Q

What Protein calorie Malnutrition?

-inadequate protein with sufficient kcal. generally the result of a diet high in grains and deficient in protein
-symptoms: edema of belly, legs
- seen in developing countries, burn patients, following major surgery
- prone to infection, rapid heart rate, excess fluid in lungs, pneumonia, septicemia, and water and electrolyte imbalances

A

Kwashiorkor

96
Q

What Protein calorie Malnutrition?

-severe deficiency in kcal
- symptoms: wasting
-misnomer: deficiency of all nutrients
-body temp and blood pressure are low
-prone to dehydration, infections, and unnecessary blood clotting

A

marasmus

97
Q

what factors compose metabolic wasting?

A

increased use of protein for energy
decreased synthesis of hair/skin pigments
decreased immunoglobin synthesis
decreased synthesis of transport proteins

98
Q

Age-associated loss of muscle mass
approx .5%/yr between ages 30-50 and 1-2% after
reduced muscle function results in increased risk of falls, disability, frailty
causes: age-related loss of moto neuron input to muscle; oxidative stress; reduced testosterone; reduced dietary protein intake
-effects mitigated by adequate protein intake and physical activity

A

sarcopenia

99
Q

what are some risks to a high protein diet?

A

dehydration
renal damage (with pre-existing conditions

100
Q

what are some benefits to a high protein diet?

A

muscle growth (with resistance exercising)
possible weight loss

101
Q

A group of organic chemicals in which one or more hydroxyl (OH) groups are attached to the carbon atoms in place of the hydrogen atoms

A

alcohol

102
Q

ethyl alcohol; found in alcoholic beverages
- considered safe for consumption
- excess can be toxic, can damage the body, and can be lethal

A

ethanol

103
Q

sugar alcohol; found in food and in the body as part of the triglyceride molecule

A

glycerol

104
Q

alcohol found in antifreeze
- poisonous

A

methanol

105
Q

alcohol found in rubbing alcohol
- poisonous

A

isopropanol

106
Q

metabolic process that converts sugar in grains and fruit (e.g., glucose, maltose, fructose) to acids, gases, and/or alcohol by the action of yeast and bacterias

A

Fermentation

107
Q

forms liquors
-fermented liquid is heated and ethanol vaporizes
-vapors are collected and form liquor
- alcohol content is indicated by its proof

A

Distillation

108
Q

how much average alcohol does the body produce via fermentation per day?

A

approx 3 g of ethanol

109
Q

Does alcohol require digestion?

A

No

110
Q

How is alcohol absorbed?

A

simple diffusion

111
Q

Where is most of the alcohol absorbed?

A

small intestine

112
Q

Where is alcohol metabolized?

A

some in the stomach
most transported via blood stream to liver

113
Q

What are the three metabolic pathways alcohol primarily metabolizes through?

A
  1. Alcohol Dehydrogenase (ADH) pathway
  2. The microsomal ethanol oxidizing system (MEOS)
  3. Catalase System
114
Q

What alcohol metabolic pathway does this describe?
-present in stomach and liver
- metabolizes large majority of alcohol consumed
- converts alcohol to acetyl CoA
*used to produce energy in TCA cycle
*converted into fatty acids and stored as a triglyceride

A

Alcohol dehydrogenase pathway (ADH)

115
Q

In the ADH pathway, What enzyme converts ethanol to acetaldehyde and located in the liver?

A

alcohol dehydrogenase

116
Q

In the ADH pathway, what enzyme transforms acetaldehyde into acetate?

A

acetaldehyde dehydrogenase

117
Q

In the ADH pathway, What is the final step in the metabolism of ethanol?

A

to convert acetate into acetyl CoA

118
Q

What does the buildup of NADH from drinking too much alcohol result in?

A

the formation of fatty acids and ketones

119
Q

What alcohol metabolic pathway does this describe?

  • used when there is too much alcohol and ADH cannot keep up; and/or with chronic alcohol consumption
  • metabolize alcohol to acetaldehyde via an oxidase enzyme (CYP2E1, part of the cytochrome P450 family)
  • occurs in liver and extra-hepatic tissues, including the brain
  • used to metabolize drugs and other foreign compounds, but alcohol takes precedence over drugs, thus consumed together can cause lethal doses of drugs in the blood (e.g. acetaminophen)
A

The Microsomal ethanol Oxidizing System

(MEOS)

120
Q

What system is activated with chronic alcohol consumption, resulting in enhanced alcohol tolerance?

A

The Microsomal ethanol Oxidizing System

(MEOS)

121
Q

What alcohol metabolic pathway does this describe?

  • metabolizes alcohol into acetaldehyde
  • hydrogen peroxide is necessary
  • quantitatively, this system is considered a minor pathway of alcohol oxidation, but may play a large role in alcohol metabolism in the brain
A

Catalase System

122
Q

about how many drinks can the liver metabolize in an hour?

A

1 but this rate varies by up to 3 fold

123
Q

What happens to excess alcohol that is not metabolized via “first pass”?

A

circulates throughout the body and raises blood alcohol concentration (BAC)

124
Q

True or False
amount of alcohol expelled throughout the lungs correlates with the amount of alcohol in the blood

A

True

125
Q

Full stomach reduces alcohol absorption speed and can reduce BAC by up to __%

A

50%

126
Q

Females have __% less ADH than males

A

20-30%

127
Q

Lower ADH =

A

lower alcohol tolerance

128
Q

Lower ALDH =

A

severe hangovers

Human Nutrition (5 decks)

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