Protein Nutrition, Digestion, absorption Flashcards

1
Q

What determines the function of an amino acid

A

The variable ‘R group’

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2
Q

What makes up an amino acid?

A

amino group, acid group, R group, H

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3
Q

Non-essential amino acids are?

A

we can make, either from essential aa or derive from other metabolic components

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4
Q

Essential aa are?

A

Required in our diet, we can’t make ourselves

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5
Q

Roles of Proteins? (8)

A
  • building material
  • hormones
  • enzymes (digestive)
  • immune function
  • fluid balance
  • Transporters
  • AB
  • Energy source
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6
Q

Conditionally Essential aa

A

When the thing that makes the aa has to be avoided, so nonessential aa become essential

Phenile pertenuria: have to avoid phenilalinine, can’t make tyrosin

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7
Q

Bonds of proteins

A

peptide bonds (OH + H)

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8
Q

Polypeptides function due to?

A

Their sequencing of aa, determined by DNA/RNA

eg) haemoglobin (4pp bound)
if aa sequence altered, the protein can’t function > Sickle cell anaemia

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9
Q

Main victims of Protein-energy malnutrition

A

Children

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10
Q

what is the protein RDI? Total energy intake? Is this attainable?

A

M: 0.84g/kg/day
F: 0.75g/kg/day

12-25% of energy intake

This is very easy to achieve

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11
Q

Is taking protein supplements always necessary? What can this lead to

A

No. its very easy to achieve RDI, so you are getting excessive amounts of protein. Even when you are active, and your protein turnover is higher.
Potential links with CVD and renal stones?

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12
Q

High Quality Protein?

A

Provide enough of all the EAA
Meats do this
But vegans/vegetarians need to find other sources (supplements etc)

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13
Q

Difference in digestibility of proteins?

A

animal protein: 99%
plant protein: 70-90%
soy & legumes: 90%

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14
Q

Amino Acid composition means

A

Dietary protein must supply minimum
9EAA + N containing amino groups + energy

if there is not enough EAA synthesis limited

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15
Q

Recommended serving of protein?

A

1-2 per day of MIXED servings. By combing protein sources its easy to get EAA

Complementary proteins (provide SOME of the EAA)

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16
Q

Protein digestion in the mouth

A

mouth and salivary glands chew, crush and moisten protein-rich foods and mix them with saliva

17
Q

Protein digestion in the stomach

A

Acid environment denatures proteins and actives pepsinogen > pepsin.
HCl: uncoats protein strands and activates stomach enzymes
Pepsin: cleaves proteins > smaller polypeptides and some free aa. Inhibits pepsinogen synthesis

18
Q

Protein digestion in the SI

A

Degraded by a combo of pancreatic endopeptidases. (trypsin, chymotrypsin, elastase)
Polypeps &raquo_space;» smaller polypeptides and amino acids

Then pancreas enzymes (intestinal tri/di peptidases) of the surface of enterocytes hydrolyse these and they are absorbed

Peptides&raquo_space;» amino acids

19
Q

What initiates protein digestion in the SI to occur. What happens next?

A

Trypsinogen&raquo_space; Trypsin
by membrane -bound enteropeptidases
Trypsin (when high enough) has a negative feedback on trypsinogeen synthesis. It activates inactive enzymes such as chymotrypsinogen to their active form.

These active enzymes can now cleave off aa chains to make them absorbable.

20
Q

Absorption of Proteins works by?

A

peptides/ aa absorbed through gut enterocytes, facilitated by either Na+ or H+ co-transporter.

A antiport in the BL membrane swaps Na+ for K+ and creates the necessary conc gradient

Larger peptides can be transcytosed and engulfed into membrane

venule > villi > portal vein > liver

21
Q

Does digestion occur in the enterocytes?

A

Yes of di/tripeptides

22
Q

Downside of using protein as energy?

A

Ammonia and urea.

These are toxic and need to be excreted

23
Q

Nitrogen balance?

A
  • Usually in nitrogen balance (protein/nitrogen intake = protein/nitrogen excretion)
  • Nitrogen is taken into the body largely as aa.
  • Majority excreted via urine as N products
  • This is relatively stable over a wide range 50-300g
24
Q

g Protein =

A

gN x 6.25

25
Q

Negative Nitrogen balance? Factors that cause this?

A

Net loss of Nitrogen.

1) Decreased protein intake
2) starvation or decreased GI function
3) injury, trauma, burns (not enough protein> tissue damage leads to death)
4) illness or infection
5) some post-op conditions
6) many cancers
7) lactation

26
Q

Positive Nitrogen balance. Factors that produce this.

A

Net gain of Nitrogen (synthesis> degredation)

1) increased protein intake
2) growth
3) pregnancy
4) recovery from illness/ trauma

Only for a short period, body quickly excretes

27
Q

PEM stands for

A

Protein-Energy Malnutrition

occurs in developing countries, especially children

28
Q

Why is malnutrition so dangerous in children

A

Leaves them vulnerable to infection&raquo_space; low food makes infection worse&raquo_space; hard to get them too eat when infection develops death

29
Q

Two main forms of PEM

A

1) Marasmus

2) Kwashiorkor

30
Q

Marasmus (like anorexia nervosa)

A
  • Severe deprivation or impaired absorption of protein, energy, vitamins, minerals.
  • Slowly develops
  • Leads to severe weight loss, muscle-wastage, no body-fat, growth
31
Q

Why is it interesting that marasmus sufferers don’t have oedema

A

If we got sick and decreased protein intact we would develop oedema, but this chronic malnutrition is different

32
Q

Kwashiokor

A

infants and young children, more acute/rapid onset

  • due to protein shortage or infection
  • Some weight loss, some muscle wastage, some body fat
  • 60-80% growth for age
  • edma (fat tummy) , fatty lliver
  • Anxiety, apathy, sadness
  • Appetite loss
  • hair dry, brittle, skin gets lesions