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Advanced Nutrition: Proteins, Vitamins, and Minerals > Introductory Concepts > Flashcards

Introductory Concepts Flashcards

1
Q

What is a distinguishing factor of Protein in Comparison to the other macronutrients?

A

Contains Nitrogen

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2
Q

Protein is a major ______ and _______ component of all cells

A

functional and structural

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3
Q

Protein in the human body is used for

A

1) All enzymes
2) Membrane components and carriers
3) Blood transport molecules
4) Intracellular matrices
5) Muscle, bone, skin, hair, fingernails
6) Keratin, collagen
7) Some hormones

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4
Q

The largest energy store in the body is ________.

A

Fat

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5
Q

The components of the body listed from highest to lowest is:

A

Body and Water Minerals –> Fat –> Protein –> Glycogen

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6
Q

Does fat or protein provide more energy?

A

Fat

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7
Q

What is the bioavailability in days of protein?

A

13 days

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8
Q

Can you use up all of your protein stores?

A

No, you would die

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9
Q

Humans eat protein, but need ________

A

amino acids

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10
Q

How many amino acids are there?

A

hundreds

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11
Q

α-amino acids except for proline (α-imino)

A

1) 20 with cognate tRNA

2) tRNA for selenocysteine

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12
Q

What is post transcription?

A

Adding a hydroxy or methyl group after the AA becomes apart of the chain

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13
Q

Most of our amino acids are what kind of amino acids?

A

α-AA

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14
Q

Non-Protein α-AA’s (6)

A 
Ornithine
Citruline
Homocysteine
Hydroxylysine
Hydroxyproline
3-methyl-histidine
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15
Q

Not an α-AA

A

Taurine

beta-alanine

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16
Q

Protein contains ______ % Nitrogen by weight

A

16%

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17
Q

Weigh ratio of protein/nitrogen (p/n)

A

6.25

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18
Q

100g protein = 16g nitrogen
100/16 = 6.25
So,

Nitrogen (g) x 6.25 = _________

A

Grams of Protein

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19
Q

Amino acids are linked together via ______ to form _____

A

Peptide Bonds(linkages), Peptide Chains

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20
Q

Protein Structure can be

A

Primary

Secondary

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21
Q

A Secondary Protein Structure forms a ______ ______

A

double helix

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22
Q

Why does a helical structure form?

A

The hydrogen bonds are not very strong, so it results in a winding structure

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23
Q

The Amino end is also called the __ - _____ ____ and is on the ______ side

A

N-terminal end, left

H3N+

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24
Q

The Carboxyl end is also called the __ - _____ ____ and is on the ______ side

A

C-terminal end, Right

COOH
C=0
=0-

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25
Q

The total effect of AA’s is ______

A

neutral

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26
Q

Peptide bonds form between….

A

Carboxyl group of one AA and the Amino group of another AA

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27
Q

__ - Amino acids are of nutritional significance

A

L

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28
Q

Indispensable (essential) AA’s

A

Need to attain from diet

Isoleucine (Ile)
Leucine (Leu)
Lysine (Lys)
Methionine (Met)
Phenylalanine (Phe)
Threonine (Thr)
Tryptophan (Trp)
Valine (Val)
Histidine*(His)
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29
Q

Dispensable (non-essential)

A

Can be synthesized in the body

Alanine (Ala), 
Arginine (Arg), 
Aspartic acid (Asp) 
Asparagine (Asn)
Glutamic acid (Glu)
Glytamine (Gln)
Glycine (Gly) 
Proline (Pro)
Serine (Ser)
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30
Q

Conditionally dispensable

A

Synthesis may be limited under special physiological conditions

Cysteine (Cys)
Tyrosine (Tyr)

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31
Q

Hadaad Notes

A

Structural formulas of the 21 common α-amino acids.

The α-amino acids all have a carboxyl group, an amino group, and a differentiating functional group attached to the α-carbon.

The generic structure of amino acids is shown in the upper left corner with the differentiating functional group marked by R.

The functional group for each amino acid is shown below. Amino acids have been grouped by functional class.

Proline is actually an imino acid because of its cyclic structure involving its nitrogen (N).

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32
Q

What is the structure of Amino Acids

A

1) α-amino group (NH2)
2) α-carboxyl (COOH)
3) Side Chain (R)

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33
Q

Neutral (non-polar AA)

4

A

Glycine (Gly) (3 sections) - Alanine (Ala)

Serine (Ser) - Threonine (Thr): Both have an OH group, but Thr has an extra branch

Glycine is the simplest

Threonine = secondary alcohol because the main CHCH has two branches coming off of it

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34
Q

Neutral non-polar Branched AA)

3

A

BCAA’s: serve as an energy source for muscle, all essential

Isoleucine (Ile): 5 carbon chain, not a “V” branch

Valine (Val): If turn your head on teh side it forms a “V” shape, but also has a NH2, 3 carbon chain

Leucine: Almost the same as Valine, but its downward branch has an NH3, 4 carbon chain

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35
Q

Sulfer Amino Acids

2

A

Contain a Sulfer!

Cysteine (Cys): Conditional, “HS” on the amino end

Methionine (Met): Secondary thiol, S is sandwiched between CH3 and CH2CH2CH

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36
Q

Aromatic Amino Acids (Phenols)

A

Contain a Benzene ring structure (C6H5OH) .The molecule consists of a phenyl group (−C6H5) bonded to a hydroxyl group (−OH)

Phenylalanine (Phe):

Tyrosine (Tyr): Same as Phe, but has a hydroxyl group

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37
Q

Phe and Tyr have what kind of ring?

A

Phenol Ring

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38
Q

Aromatic Amino Acids: Tryptophan (Trp)

A

Indole ring (double ring)

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39
Q

Aromatic Amino Acids: Histidine (His)

A
  • Imidazole ring
  • One ring present with two double bonds

Formula (CH)2N(NH)CH

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40
Q

What are all of the Aromatic AA’s?

4

A

Phe
Tyr
Trp
His

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41
Q

Basic Amino Acids

2

A

When put in water they become more Basic

Lysine (Lys):

  - primary amine
  - straight chain with one NH2 downward branch

Arginine (Arg):
- Has a guanidino group
- H2N – C –NH
(downward form C is a = NH2+)

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42
Q

Body Protein Reserves

A 
Skeletal muscle:	43%
Skin:			15%
Blood:			15%
Viscera (liver, kidneys) organs:10%
Rest in brain, lung, heart, etc
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43
Q

50 % of total protein in the body is in the following forms:

A

1) Collagen
2) Myosin and actin
3) Hemoglobin

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44
Q

Collagen

A

Structure of connective tissue of skin & bone

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45
Q

Myosin and Actin

A

Proteins in muscle

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46
Q

Hemoglobin

A

Blood

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47
Q

Acidic amino acids and their amides

A
  • Glutamic acid (glutamate) is longer than Aspartic acid (aspartate)
  • Glutamate –> Glutamine
  • Aspartate –> Asparagine

This occurs when the acid form takes up an amino group

  • Acidic amino acids have 2 carboxyl groups, one at each end
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48
Q

What is protein turnover?

A
  • Body proteins are constantly being synthesized and then degraded
  • In healthy adults, the total amount of protein in the body remains constant
  • The rate of protein synthesis sufficient to replace the protein that is degraded is protein turnover
  • Plasma proteins and most intracellular proteins are rapidly degraded (1/2 life = hours to days). Extracellular structural proteins such as collagen are metabolically stable and have half-lives of years.

EXTRA:
Albumin, Transferrin have a short half life and are broken down faster
- Proteins in muscle may have a longer half life
- Protein turnover mostly happens in visceral
Turnover = about 250g per day

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49
Q

Amino Acid Pool

A

1) The free amino acids distributed throughout the body
- Intracellular
- Extracellular: Blood, fluid between cell

2) The amino acid pool contains about 90 - 100 g of amino acids

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50
Q

How much protein is digested and absorbed per day?

A
  • Protein intake (dietary) = 90 g (70-100g)
  • Secreted protein or endogenous (from body to gut) = 70 g (35-200g)
  • Absorbed = 150 g
  • Fecal loss = 10 g (6-12g)
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51
Q

What two types of cells does the stomach contain?

A

Secrete Chief cells and Parietal (oxyntic) cells

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52
Q

What do chief cells secrete in the stomach?

A

pepsinogen, which is an inactive form: zymogen

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53
Q

What do parietal (oxyntic) cells secrete in the stomach?

A 
HCl  (pH 2-3)
  - Denatures protein
    - Kills microorganisms
    - Activates pepsinogen --> pepsin (active form(
Intrinsic factor
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54
Q

What percent of protein digestion occurs in the stomach

A

about 10-20%

  • Results in oligopeptides, polypeptides and amino acids
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55
Q

Most protein digestion results from the action of

A

pancreatic proteolytic enzymes

Hadaad Notes:
The proteolytic enzymes are all secreted in an inactive form, to prevent auto-digestion, and are activated in the lumen of the gut: by HCl in the case of stomach pepsinogen and by enteropeptidase and trypsin in the case of the pancreatic enzymes.

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56
Q

What stimulates the pancreas to secrete its enzymes?

A

The intestinal endocrine cells secrete:

Cholecystokinin (CCK) and Secretin

     -CCK and secretin stimulate the pancreas to secrete -   
     the protein digesting enzymes. However, the   -   
     pancreatic enzymes are secreted as zymogens 
      (inactive forms) such as trypsinogen, 
      chmotrypsinogen, proelastase, procarboxypeptidase, 
      etc.
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57
Q

How are the pancreatic enzymes activated?

A

CCK stimulates the mucosal epithelial cells to secrete enteropeptidase which which activates trypsinogen to trypsin. The other pancreatic enzymes are activated by trypsin

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58
Q

Brush border enzymes (intestinal peptidases)

    The intestinal brush border has: \_\_\_\_\_, \_\_\_\_\_, \_\_\_\_
A

Dipeptidases
Tripeptidases, and
Aminopeptidases

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59
Q

Brush border enzymes (intestinal peptidases)

    Absorption of peptides and whole proteins
A

Rare

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60
Q

Brush border enzymes (intestinal peptidases)

 \_\_\_\_\_\_ peptides may be absorbed intact and hydrolyzed within intestinal cell
A

Small

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61
Q

Action of Peptidases: Endopeptidases

A

Hydrolyze bond (cleave) in the middle of the chiain

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62
Q

Action of Peptidases: Exopeptidases

A

Hydrolyze bond (cleave) at the terminal end of the chain, either at the Aminopeptidase end of the caboxypeptidase end

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63
Q

Transport (absorption) of amino acids: Transport systems

What are amino acid transporters?

A

Membrane bound proteins that recognize different amino acids and move them into and out of cells

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64
Q

Transport (absorption) of amino acids: Transport systems

The ______ _______ and ______ _______have common transport systems

A

Small intestine and Kidney Tubules

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65
Q

What are the two types of Transport Systems?

A

1) Sodium independent

2) Sodium dependent
-Co-transport (secondary active transport) of amino acids
and peptides

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66
Q

Hadaads Notes on: Transport and absorption of amino acids and peptides

1) How are amino acids mostly absorbed?
2) How are Di-peptides and tri-peptides transported?
3) How are some large peptides or protein can be carried across the cell

A

1) By sodium dependent co-transporters.
2) By a H+ ion dependent co-transporter

3) Transcytosis
- This is particularly true in babies and is a mechanism
whereby the immunoglobulins in mothers milk can be
transfered to the child.

67
Q

About how much protein is degraded (broken down) per day?

A

250-300g per day

The proteins that are broken down are typically the ones that are damaged or not needed anymore

68
Q

Why is protein degradation (breakdown) important?

A

1) Cell growth
2) Adaptation to different physiological conditions
3) Elimination of abnormal or damaged protein
4) Normal functioning of the immune system

69
Q

What are the two pathways of Protein degradation?

A

Lysosome and Ubiquitin-proteasome pathways

70
Q

Lysosome pathways

1) Energy ________
2) Contains acidic ______
3) Breaks down ______

A

1) indepedent
2) enzymes
3) proteins

Lysosomes have digestive enzymes in them which take damaged/bad proteins and digests them. AA’s are produces and goes to cytoplasm of cell

71
Q

Where does protein degradation happen?

A

Inside the cell (intracellular)

72
Q

UBP Pathways

1) Energy ________
2) Notes

A

1) dependent
2) Damaged or unneeded proteins are marked for destruction by covalent attachment to a small protein called ubiquitin.
- Polyubiquinated proteins are degraded by intracellular proteosomes
- This system degrades abnormal proteins, normal proteins and proteins of the endoplasmic reticulum

73
Q

What is UBP pathway activated (+) by? (2)

A

1) Fasting (not eating)

2) Hormones

74
Q

What is UBP pathway activated (-) by? (2)

A

1) Feeding and increased protein intake

2 )Hormones (insulin, growth factors)

75
Q

What hormones activate (+) UBP Pathways?

A

glucagon, glucocorticoids, thyroxin

76
Q

What hormones activate (-) UBP Pathways?

A

insulin, growth factors

77
Q

What are the Physiological roles of dietary proteins and amino acids? (4)

A

1) Protein synthesis

2) Synthesis of nitrogen containing molecules
- Dispensable amino acids
- Enzymes, nucleic acids, hormones, neurotransmitters,
etc.

3) Provide energy (ATP) from “carbon skeleton”
- Oxidation of “carbon skeletons” to: energy + CO2 +
H2O
- Amino group is excreted as urea and ammonia

4) Provide amino acids for conversion to:
- Acetyl CoA –> fats and sterols
- Carbohydrate intermediates –> glycogen

78
Q

Amino Acids can also be broken down and used for _______.

A

Energy

Extra: Amino Acids are used not only for synthesis, but also for energy (ATP) from the carbon skeleton

79
Q

What does the breakdown of Amino Acids begin with?

What types of reactions follow? (3)

A

The removal of the amine group mainly by the following types of reactions:

1) Transamination (all tissues)
2) Oxidative Deamination
3) Synthesis and hydrolysis of gluatamine

80
Q

Transamination

A

Transamination (all tissues)  the funneling of amino groups to glutamate

 -Enzymes are called transaminases (also called   
  aminotransferases)

 - Transaminases use pyridoxal phosphate (PLP) as    
   cofactor

  - The keto acid α-ketoglutarate accepts amino groups      
  from most amino acids to produce glutamate
81
Q

Transamination Hadaad Notes

A

Transamination (or aminotransfer) is a chemical reaction between two molecules. One is an amino acid, which contains an amine (NH2) group. The other is a keto acid, which contains a keto (=O) group. In transamination, the NH2 group on one molecule is exchanged with the =O group on the other molecule. The amino acid becomes a keto acid, and the keto acid becomes an amino acid.
Transamination in biochemistry is accomplished by enzymes called transaminases or aminotransferases. This process is an important step in the synthesis of some non-essential amino acids (amino acids that can be synthesized de novo by the organism). Transamination reactions use the coenzyme PLP, and has been shown to be a kinetically perfect reaction. The product of transamination reactions depend on the availability of alpha-keto acids. The products usually are either alanine, aspartate or glutamate, since their corresponding alpha-keto acids are produced through metabolism of fuels.

82
Q

What happens in oxidative deamination?

A

Enzyme glutamate dehydrogenase converts glutamate to α-ketoglutarate and ammonia

83
Q

What happens in the Synthesis and hydrolysis of glutamine?

A

Enzyme glutaminase hydrolyzes glutamine to produce glutamic acid and ammonia

84
Q

What are the 2 important transamination reactions?

A

1) Reaction catalyzed by ALANINE TRANSAMINASE (ALT)

2) Reaction catalyzed by ASPARTATE TRANSAMINASE (ASP)

85
Q

Alanine Transaminase Reaction (ALT)

The enzyme ____________ catalyzes the transfer of the amino group of alanine to ________ resulting in the formation of ________ and ________ .

Is this reaction reversible?

A

1) alanine transaminase
2) α-ketoglutarate
3) pyruvate and glutamate

Yes, The reaction is reversible, but during amino acid catabolism, the enzyme functions in the direction of glutamate synthesis. Thus glutamate, acts as a collector of nitrogen from alanine.

86
Q

Aspartate transaminase (AST)

Aspartate transaminase transfers amino groups from glutamate to _______ to form ________,

Asparate is used as a source of nitrogen in the ___ cycle

A

1) oxaloacetate
2) aspartate
3) urea

87
Q

ALT

A

Alanine –> α-ketoglutarate = pyruvate and glutamate

88
Q

In ALT, glutamate acts as a collector of _____ from alanine

A

nitrogen

89
Q

AST

A

Glutamate –> OAA –> Aspartate = Nitrogen used in urea cycle

90
Q

Amino form: Alanine

A

Keto form: Pyruvate

91
Q

Amino form: Aspartic Acid

A

Keto form: OAA

92
Q

Amino form: Glutamic Acid

A

Keto form: α-ketoglutarate

93
Q

Amino form: Leucine (BCAA)

A

Keto form: α-ketoisocaproic acid (BCAA keto-acid)

94
Q

What is removed in Oxidative Deamination?

A

Amino group

95
Q

Where does Oxidative Deamination occur?

A

Liver and Kidney

96
Q

What catalyzes Oxidative Deamination?

A

glutamate dehydrogenase

97
Q

What is released as a result of Oxidative Deamination?

A

Ammonia (NH3)

  • Amino group is removed entirely as ammonia
98
Q

What must be present for Oxidative Deamination to happen?

A

NAD, thus it requires energy

99
Q

What are the end products of Oxidative Deamination?

A

α-ketoglutarate and ammonia

100
Q

Synthesis and hydrolysis of gluatmine is the removal of ______ ____ __

A

Amino acid Nitrogen (N)

101
Q

What enzyme synthesizes glutamine (Gln)

A

glutamine synthetase

102
Q

What does glutamine synthetase do?

A

Adds ammonia to glutamate = glutamine

103
Q

Where does the synthesis of glutamine occur?

A

Most tissues

104
Q

Where does the hydrolysis of Glutamine (Gln) occur?

A

Liver

105
Q

What enzyme is used for the hydrolysis of Glutamine (Gln)

A

glutaminase

106
Q

What does glutaminase do?

A

Coverts Glutamine –> glutamate + free ammonia

107
Q

How is Glutamine degraded back to glutamate?

A

Liberation of the amide-N to release ammonia by a different enzymatic pathway (glutaminase). NH3, ammonia.

108
Q

In the Urea cycle, What is the major disposal form of NH3

A

Urea

109
Q

In the Urea cycle, Where is NH3 generated (via glutamate dehydrogenase)?

A

Mitochondria

110
Q

In the Urea cycle, Where does the first reaction of the Urea cycle take place?

A

Mitochondria

111
Q

In the Urea cycle, amino groups of many amino acids are transferred primarily to ____________

A

α-ketoglutarate (in skeletal muscle to pyruvate)

112
Q

In the Urea cycle, what 2 amino acids are transported via the blood to the liver, where they are deaminated to form ammonia

A

glutamate and alanine

113
Q

In the Urea cycle, Where do the 2 Urea N groups come from?

A

One comes from free NH3 (from oxidative deamination of glutamate)

One comes from aspartate (which got it from glutamate)

114
Q

In the Urea cycle, Glutamate is the primary source for the

A

Aspartate N

115
Q

In the Urea Cycle, glutamate is also an important source of the _________ into the cycle.

A

ammonia

116
Q

Approximate distribution of nitrogen in urine in human consuming 100 g of protein per day is

A

16g N

117
Q

If a person has 12.8g N (i.e. from Urea) per day, you multiply that by ________ to = g of _______

A

6.25, protein

118
Q

What are the 4 sources of ammonia? aka where does ammonia come from

A

1) Amino acids
- glutamate dehydrogenase

2) Glutamine and other amides
- glutaminase

3) Nucleic acids
4) Bacterial UREASE in intestine

119
Q

How is extra Nitrogen disposed? aka How do we get rid of ammonia from our bodies?

A

1) Formation of urea

2) Excretion by kidney as ammonia (acid-base balance)

120
Q

Define Glucogenic

A

Yield pyruvate or one of the intermediates of the citric acid cycle

121
Q

Define Ketogenic

A

Yield acetyl-CoA or intermediates of fatty acid oxidation

122
Q

What AA is purely ketogenic?

A

Leucine

123
Q

What AA’s are both ketogenic and glucogenic?

A

Ile, Lys, Phe, Tyr, Trp

124
Q

What AA’s are purely glucogenic?

A

alanine, serine, glycine, cysteine, aspartic acid, asparagine, glutamic acid, glutamine, arginine, histidine, valine, threonine, methionine, proline

125
Q

What is the intestinal tract lined with?

A

Continuous layer of epithelial cells

126
Q

What is the Is the largest lymphoid organ in the body (gut associated lymphoid tissue)?

A

Intestinal Tract

127
Q

What are the major fuels for the small intestinal mucosa?

Which 3?

A

Dietary AA’s

glutamine, glutamate, aspartate

128
Q

Dietary Amino Acids

A

1) Are major fuels for the small intestinal mucosa (glutamine, glutamate, aspartate)
2) Are substrates for synthesis of intestinal
3) Show trophic and cytoprotective effects on gut integrity
4) Show potential therapeutic applications

129
Q

In regards to proteins, the gut accounts for __- __% of whole-body protein synthesis

A

9-12%

130
Q

In regards to dietary amino acids

what are Are substrates for synthesis of intestinal
1) Proteins (gut accounts for 9-12% of whole-body
_______ synthesis

   2) Nitric oxide (\_\_\_\_\_\_\_)
  3) Polyamines (putrescine, spermidine, etc. (\_\_\_\_\_\_)
   4) Glycoproteins (\_\_\_\_\_\_\_) 
   5) Ornithine, citrulline, and arginine (from \_\_\_\_\_\_\_)
A

1) protein
2) arginine
3) from arginine
4) threonine, found in mucous
5) proline

131
Q

Glycoproteins are made up of ______ and ______

A

protein and sugar

132
Q

What is an example of a FAST protein that is digested and absorbed quickly

A

Whey

133
Q

What type of protein increases satiety?

A

Whey

134
Q

What kind of protein increases protein synthesis?

A

Whey

135
Q

What is an example of a SLOW proteins that is digested and absorbed more slowly

A

Caesein

136
Q

Which type of protein allows plasma concentrations of amino acids are maintained over a longer period of time

A

Caesein

137
Q

After protein is ingested, it is absorption from the small intestines into the _______ _________

A

Portal circulation

138
Q

Which organ is in charge of distribution and control of blood concentrations?

A

Liver

139
Q

After protein is ingested, utilization by cells for protein synthesis depend on what 3 things?

A

1) Quality of protein
2) Size of meals
3) Slow and fast proteins

140
Q

____ and _______ exert different effects on plasma amino acid profiles, gastrointestinal hormone secretion and appetite.

A

Casein and Whey

141
Q

Individuals consume less calories when they are preloaded with which type of protein? Casein or Whey?

A

Whey

142
Q

Circulating concentrations of the various amino acids reflect the composition of the proteins and amino acids consumed
in which state?

A

Postprandial state

143
Q

Which state does the following describe?

  • The amino acid profile of blood is stable and characteristic of species
    - There is a net release of amino acids from muscle to
    plasma
    - There is uptake of amino acids by kidneys for
    gluconeogenesis and ammonia formation
  • Conditions which results in changes in the concentrations of amino acids in blood
    - The neonatal period
    - Catabolic and disease conditions
A

Postabsorptive

144
Q

True of False: Different animals/humans have difference postabsorptive states rates/Postabsorptive states depend on the species

A

True

145
Q

AA in the Colon

Some proteins and amino acids escape digestion and absorption and end up in the ________.

A

Colon

  • Are absorbed and metabolized by colonic cells
  • Are metabolized by bacterial flora to produce ammonia, hydrogen sulfide, amines, short-chain fatty acids
146
Q

AA in the Colon

Bacterial flora also produce ammonia from urea catalyzed by bacterial _________

A

urease

147
Q

AA in the Colon

Are amino acids synthesized de novo by gut bacteria absorbed by humans?

A

Some evidence exists

148
Q

The following are all roles of what organ?

1) Monitors absorbed amino acids and adjusts rate of metabolism according to body needs
2) Increased protein intake results in higher activity of liver enzymes which metabolize amino acids. Liver breaks down most amino acids except branched chain.

3) There is a difference in the metabolism of dispensable versus indispensable amino acids by the liver depending on the diet
- There is a direct correlation between the amount of
protein in the diet and catabolism of dispensable amino
acids
- Indispensable amino acids catabolism increases only
when the diet provides substantial amounts of those
amino acids

A

Liver

149
Q

What explains the interaction between muscles and liver cells?

A

Skeletal muscle: The alanine cycle

150
Q

Skeletal muscle: The alanine cycle

The Skeletal muscle: The alanine cycle likes to oxidize which AA’s

A

BCAA’s: Ile, Leu, and Val

151
Q

Skeletal muscle: The alanine cycle

Does the release of amino acids from muscle reflect the amino acid profile of muscle?

A

No

152
Q

Skeletal muscle: The alanine cycle

What fraction of amino acids released from muscle are alanine and glutamine?

A

2/3rds

153
Q

Skeletal muscle: The alanine cycle

_______ 1st undergo transamination and then are oxidized in muscle tissue for energy

A

BCAA’s

154
Q

Skeletal muscle: The alanine cycle

The amino groups are carried from:
alanine –> ____ and
glutamine –> ______

A

alanine –> liver
- it is then changed to glucose for energy

glutamine –> gut

155
Q

Postabsorptive state means

A

after we have eaten

156
Q

Fasting means

A

we have not eaten for a while

157
Q

The brain uses what for energy?

A

Glucose

158
Q

In a postabsortive state there is more ___ and less ___

A

more glucose

less ketones

159
Q

In a fasting state the brain oxidizes more _____ and less ______

A

more ketones

less glucose

160
Q

Ketones come from the oxidation of Ketogenic AA’s, Glycerol, and _____

A

FFA’s

161
Q

Glycerol is the backbone of _____

A

Triglycerides

162
Q

The Gut loves to use glutamate and _____

A

glutamine

163
Q

Skeletal muscle

What are the two biomarkers for meat intake?

A

3-methyl histidine and 1-methyl histidine

  • excreted in the urine
  • bodybuilders produce more because of protein turnover
  • these biomarkers result from muscle turnover and consumption of meat from the diet

Advanced Nutrition: Proteins, Vitamins, and Minerals (3 decks)

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