Protein digestion Flashcards
What are the cells of the pancreas and what do they produce?
alpha cells - glucagon
beta cells - insulin
delta cells - somatostatin
acini cells - digestive enzyme (secreted as zymogens)
What pancreatic enzymes digest protein?
Trypsin
chymotrypsin
elastase
pro-carboxypeptidase
What causes zymogens from the pancreas to be converted into active enzymes?
activated in the duodenum by enteropeptidase
What are exopeptidases and endopeptidases?
Exopeptidases - detach the terminal amino acids from polypeptide e.g., aminopeptidases
Enodpeptidases - hydrolye internal peptide bonds of a protein e.g., trypsin, pepsin, elastase
What is the action of serine endoproteases?
Synthesised by pancreatic acinar cells
secreted into SI
Chymotrypsin - cleaves bond following large hydrophobic amino acid residue e.g. tyrosine, phenylalanine
Trypsin - cleaves bonds after a +ve charged amino acid residue e.g., aginine and lysine
Elastase - cleaves bonds after a small neutral amino acid residue e.g., alanine, glycine, valine
Describe the process of protein digestion
Protein denatured by stomach acid
Passes to SI
Luminal phase - bond-specific proteases hydrolyse protein to short chain peptides
Membranous phase - hydrolysed further to di/tripeptides and some free amino acids
Specific membrane proteins transported across gut wall by secondary active transport
What is the action of aminopeptidases?
attack the amino terminal of peptides secreted from the SI
exopeptidases
Describe the routes of amino acid transport
- peptide transporter
- single amino acid transport from instestinal lumen is an active process that involves Na+ dependent carrier-mediated cotransport system. Selective carrier systems are present for certain groups of amino acids:
- neutral AAs
- acidic (dicarboxylic) AAs
- imino amino acids
- basic amino acids