Team:Imperial College London/Stomach
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Revision as of 09:15, 2 October 2009
Contents |
Human Digestive Proteases:
- Pepsin = stomach
- Trypsin = duodenum
- Chymotrypsin
- Carboxypeptidase
Stomach
The stomach is the first point at which polypeptides are broken down. The low pH of the stomach causes enzymes to denature, opening them up to attack from proteases such as pepsin.
Pepsin
- Released by chief cells in the stomach.
- Expressed as a zymogen pepsinogen.
- Pepsinogen is converted to pepsin by HCl which is released by parietal cells of the stomach.
- Cleaves at the N-terminus after aromatic amino acids such as phenylalanine, tryptophan, and tyrosine.
- Optimum pH of 1.5 to 2. Pepsin denatures when the pH is more than 5.0.
If you want to see the effect of the protease pepsin, please enter the amino acid sequence of a polpeptide into the table below.
Duodenum
Endopeptidases (trypsin, chymotryopsin, elastase)
Exopeptidases (carboxypeptidases A & B)
Enteropeptidase
Trypsin
- Trypsin is found in the duodenum and serves to hydrolyse peptides into amino acids.
- Trypsin has an optimal operating pH of ~8 and an optimum temperature of 37°C.
- Trypsin breaks down the milk protein casein. For this reason, milk protein would be a good protein to use for secondary encapsulation.
Chymotryopsin
Elastase
Enterokinase
Carboxypeptidases A & B
Small Intestine = Aminopeptidase N
Dipeptidyl aminopeptidase IV
Aminopeptidase P
Carboxypeptidase P
Angotensin-converting enzyme
Glutamyl aminopeptidase
Peptide cutter
PeptideCutter [references /
documentation]
predicts potential cleavage sites cleaved by proteases or chemicals in a given protein
sequence.
PeptideCutter returns the query sequence with the
possible cleavage sites mapped on it and /or a table of cleavage site positions.