Lecture 14 Flashcards

1
Q

What are the functions of proteins?

A
  • Building materials for growth and maintenance
  • Enzymes
  • Hormones
  • Regulators of fluid balance
  • Acid-base regulators
  • Transporters
  • Antibodies
  • Source of energy
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2
Q

What are the 24 specific organic compounds required?

A

9 essential amino acids
2 fatty acids
13 vitamins

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3
Q

What are the 9 essential amino acids?

A

His, ile, leu, lys, met, phe, thr, trp, val

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4
Q

Why are some amino acids non-essential?

A

Derived from other metabolic products

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5
Q

What is the recommended intake of protein?

A

15-25% of total energy intake

0.84g/kg for males and 0.75g/kg for females

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6
Q

What are the two factors that influence protein quality?

A

1) Digestibility: depends on source and other foods eaten with it. High for animal, less for plant.
2) Amino acid compositions: dietary protein must supply at least 9EAA plus enough N containing amino groups and energy for synthesis of others.

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7
Q

What happens to protein in the mouth?

A

Chewing and crushing moisten protein-rich foods and mix them with saliva to be swallowed.

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8
Q

What happens to protein in the stomach?

A

HCl uncoils and denatures protein strands and activates stomach enzymes (pepsinogen to pepsin):
Protein is broken down to smaller polypeptides by pepsin.

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9
Q

What happens to polypeptides in the small intestines?

A

Polypeptides get broken down to tripeptides and dipeptides and amino acids by pancreatic endopeptidases (trypsin, chymotrypsin, elastase). Intestinal tripeptidases and dipeptidases hydrolyse peptides into amino acids that are absorbed.

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10
Q

What happens to trypsinogen in the pancreas?

A

Inactive trypsinogen is converted to active trypsin by enteropeptidase

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11
Q

What are the effects of trypsin?

A
  • Inhibits trypsinogen synthesis
  • Cleaves peptide bonds
  • Converts pancreatic procarboxypeptidases to carboxypeptidases
  • Converts chymotrypsinogen to chymotrypsin and elastase
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12
Q

What exopeptidases are secreted in pancreatic juice?

A

Carboxypeptidase A and B

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13
Q

What are the transporters of the small intestine that aid in transport of proteins?

A
  • 3 Na+ linked amino acid transporters
  • H+ linked peptide transporter (di and tripeptides)
  • These symports are powered by an Na+/K+ antiport
  • Small peptides are carried intact across the cell by transcytosis
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14
Q

What percentage of protein digestion is complete when the jejunum is reached?

A

80%

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15
Q

What is meant by nitrogen balance?

A

Nitrogen intake = rate of nitrogen expenditure

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16
Q

What is nitrogen taken into the body largely as?

A

Amino acids

17
Q

What are the three states of N balance?

A

Negative, equilibrium, positive

18
Q

What is meant by negative nitrogen balance?

A

Net loss of N

Degradation exceeds synthesis

19
Q

What are the factors that can cause negative nitrogen balance?

A
  • Decreased protein intake
  • Starvation or reduced GI function
  • Injury, trauma, surgical op
  • Illness, infection or burns
  • Some post-op conditions
  • Many cancers
  • Lactation
20
Q

How can negative N balance kill people?

A

Not enough protein to repair burns and other tissue damage

21
Q

What is meant positive nitrogen balance?

A

Net gain of N

Synthesis exceeds degradation

22
Q

What are the factors that can cause positive N balance?

A
  • Increased protein intake
  • Growth
  • Pregnancy
  • Recovery from illness or trauma
23
Q

How can an increase or decrease in protein intake be measured as?

A

Increase or decrease in protein intake causes a corresponding increase or decrease in oxidation and hence N losses

24
Q

What is the equation relating N and protein?

A

g N x 6.25 = g protein

25
Q

What are obligatory protein losses?

A

Even when no protein is consumed, there are obligatory urinary N losses of 3g N per day.

26
Q

What is the minimum intake of protein?

A

30-50 g of high quality protein needed to maintain N equilibrium

27
Q

What happens to amino acids in excess of the body’s requirements?

A

Cannot be readily stored so are deaminated to give ammonia and residual carbon skeletons. Ammonia is toxic so is carefully detoxified to urea.

28
Q

What are the compounds in which N is stored for excreted?

A
  • Urea
  • Uric acid
  • Creatinine
29
Q

What happens to the carbon skeletons resulting from deamination of amino acids?

A

Either oxidised to produce energy or used in gluconeogenesis or lipogenesis

30
Q

What are the two protein deficiencies?

A

Kwashiokor and Marasmus

31
Q

What is Kwashiorkor?

A

Acute shortage of particularly protein. Calorie intake is usually adequate and obtained almost solely as carbs from starchy foods.

32
Q

What are the symptoms of Kwashiorkor?

A
  • Some wasting in limbs
  • Protruding belly (edema around liver)
  • Some weight loss
  • Enlarged fatty liver
  • Loss of appetite
  • Hair is sparse, thin, dry
  • Skin lesions
33
Q

What is Marasmus?

A

Frank starvation, hunger and grossly inadequate diet. Also known as protein calorie malnutrition. Chronic condition.

34
Q

What are the symptoms of Marasmus?

A
  • Severe chronic weight loss
  • No detectable edema
  • Difficult to refeed because no appetite
  • Hair is sparse, thin, dry
35
Q

What is a primary cause of protein deficiency in non third-world countries?

A

Alcoholism