W5 : Proteins Flashcards
Even before digestion, protein undergoes changes when cooking. How does cooking change the conformation of protein and thus affect its bioavailability?
- Disruption of stability of tertiary/quaternary structure
- Protein uncoils and loose shape (denature)
- Improves accessibility to proteases during digestion, therefore increasing bioavailability
Protein digestion
In the stomach, what does protein get digested into, and what enzyme(s) are involved?
Pepsinogen gets activated into pepsin, and pepsin cleaves proteins into smaller polypeptides and some free amino acids
Protein digestion
In the small intestine, what is protein digested into and what enzymes are involved?
- trypsinogen activated into trypsin (secreted by pancreas) by enteropeptidase – digests polypeptide (protein) into smaller peptides
- intestinal tripeptidases – digest tripeptides into amino acids
- intestinal dipeptidases – digest dipeptides into amino acids
- intestinal aminopeptidases – removes amino acids one by one from the N-terminus of the peptide chain.
protein absorption
How are proteins absorbed in the intestine?
Intestinal cells directly absorb the amino acidsinto blood stream (blood capillaries of villi), or absorb small peptides which then get broken down by intracellular peptidases
Where are unabsorbed amino acids transported to?
Liver
What is the equation for nitrogen balance?
Nitrogen balance = nitrogen intake - nitrogen excreted
Under what situations will one have a
(i) positive nitrogen balance
(ii) equilibrium nitrogen balance
(iii) negative nitrogen balance
(i) when one retains more nitrogen than one excretes, for muscle building (e.g. body builders / pregnant women to have amino acids for baby)
(ii) Normal person
(iii) nitrogen retained < nitrogen excreted. When one is ill / when one is malnutritioned, body starts breaking down muscle protein / when one consumes low quality protein and does not have all the essential amino acids, body break down muscle
What process do extra amino acids undergo?
Deamination
What is deanimation and where does it occur?
Removal of nitrogen containing amino group from protein to produce ammonia + keto acid.
Occurs in liver
Amino acids can undergo deamination to give keto acids and ammonia.
What other 4 purposes can keto acids have, other than being involved in synthesis of non-essential amino acids?
- Production of ketones
- Metabolised for energy
- Production of glucose (carbon backbone) – gluconeogensis
- Production of cholesterol
Amino acids can also undergo transamination. What does transamination mean?
transferof an amino group to a keto acid to form new non-essential amino acids.
In what 2 ways can non-essential amino acids be formed through transamination?
.
- Keto acids from deamination + NH3 → amino acid
- amino acid 1 + keto acid 2 → keto acid 1 + amino acid 2
(amino group from amino acid 1 transferred to keto acid 2)
For excretion, ammonia is converted into ____ in the ____
Write the equation on how ____ is converted into ____.
urea, liver
2 ammonia + CO2 - H2O → urea
After liver produces urea, how is it excreted?
Urea is transported into the bloodstream to the kidneys.
Kidneys undergo ultrafiltration to filter urea out of blood.
When the liver is malfunctioning, there is high concentration of what substance in the bloodstream?
Ammonia (bc liver doesnt convert ammonia into urea effectively)
Transamination requires which Vitamin as a coenzyme?
Vit B6