Lecture 14 Flashcards
What are the roles of proteins?
- Building material.
- Hormones.
- Enzymes - digestive.
- Immune function.
- Fluid balance.
- Transporters.
- Antibodies.
- Source of energy.
What are proteins made of?
Amino acids: nonessential amino acids and essential amino acids.
There is a: acid group, amino group, alpha hydrogen and side group (R group).
What are the 9 essential amino acids?
- Histidine (his)
- Isoleucine (ile)
- Leucine (leu)
- Lysine (lys)
- Methionine (met)
- Phenylalanine (phe)
- Threonine (thr)
- Tryptophan (trp)
- Valine (val)
What are essential amino acids?
Amino acids that we cannot make in our body or derive from other metabolic products; thus we have to get them from our diet.
What are proteins?
Polypeptide - amino acids in a long chain.
What happens when sequencing of proteins goes wrong in Haemoglobin molecules?
We get sickle-cell anaemia. This is where the blood cells become sickle-shaped. Reduction in the capacity for red blood cells to carry oxygen around their body.
What is the RDI for protein?
Total = 12-25% of energy intake.
Male = 0.84g/kg/day Female = 0.75g/kg/day
What is protein quality?
High quality proteins.
Digestibility - animals vs plants.
Amino acid composition - limiting amino acid.
Describe digestion of protein in the mouth?
Chewing and crushing moisten the protein-rich foods mixed with saliva.
Describe digestion of protein in the stomach?
HCl denatures protein strands and it activates pepsinogen (pepsinogen
-> pepsin). Pepsin and HCl then turn protein into smaller polypeptides.
Describe digestion of protein in the SI?
When the pancreas secretes enzymes in the precursor form: endopeptidases (trypsin, chymotrypsin and elastase).
Polypeptides -> (endopeptidases) tripeptides, dipeptides and amino acids.
SI produces enzymes that chop the peptides into smaller amino acids.
Peptides -> (tripeptidases, dipeptidases, aminopeptidases) amino acids.
What is the key step in digestion of proteins?
Membrane-bound enteropeptidase converting inactive trypsinogen to trypsin. This will then allow trypsin to stop production of trypsinogen and to allow the enteropeptidase to activate other proteases. Thus allowing for further breakdown of polypeptides.
Describe absorption of proteins?
There are 3 Na+ linked amino-acid transporters and H+ linked peptide transporters that transport only di and tripeptides. These are powered by Na+/K+ anti porters. The amino acids enter the blood by facilitated diffusion carriers and by diffusion.
What happens to amino acids once taken up by the liver?
We are constantly turning over protein. The amount of enzymes secreted into digestive system, is reabsorbed back into the body. The amino acids -> nitrogen pool -> tissue protein. The bi-products are:
NH3 (ammonia), Urea. Don’t want the bi-products in our body.
Describe nitrogen balance?
The amount of protein we consume we excrete. Very little faecal loss of nitrogen, majority excreted via the urine.