TRYPSIN & PEPSIN

TRYPSIN

Trypsin is a  serine protease Superfamily ,  found in the digestive sytem  of many vertebrates,  where it  hydrolyse protein. Trypsin is produced in the pancrease  as the inactive prortease trypsinogen. Trypsin cleaves peptide chains mainly at the carboxyl side of the amino acid lysine or arginine. except when either is followed by proline .It is used for numerous biotechnological processes. The process is commonly referred to as trypsin proteolysis or trypsinisation, and proteins that have been digested/treated with trypsin are said to have been trypsinized.

	classification Hydrolase (o Glycosyl) weight 56303.59 molecule ALPHA-AMYLASE polymer 1 chain A organism Sus scrofa Gene name AMY2 Type protein Length 496

PEPSIN Pepsin is one of three principal protein-degrading, or proteolytic, enzymes in the digestive system, the other two being chymotrypsin and trypsin. The three enzymes were among the first to be isolated in crystalline form. During the process of digestion, these enzymes, each of which is specialized in severing links between particular types of amino acids, collaborate to break down dietary proteins into their components, i.e., peptides and amino acids, which can be readily absorbed by the intestinal lining. Pepsin is most efficient in cleaving peptide bonds between hydrophobic and preferably aromatic amino acids such as phenylalanine, tryptophan, and tyrosine.

classification Hydrolase/hydrolase Inhibitor weight 35385.97 molecule PEPSIN 3A polymer 1 chain E organism Homo sapiens Type protein Length 326