Description
Trypsin (EC 3.4.21.4) is a serine protease from the PA clan superfamily, found in the digestive system of many vertebrates, where it hydrolyses proteins. Trypsin is produced in the pancreas as the inactive protease trypsinogen. Trypsin cleaves peptide chains mainly at the carboxyl side of the amino acids 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.
Abbr
Trypsin Acetylated, Native (Bovine)
Applications
Trypsin has been used in a study to assess the ontogeny of the endocrine pancreas in the fetal/newborn baboon. Trypsin digestion and hydrogen/deuterium exchange support the transition between inward-and outward-facing conformations during the catalytic cycle of the bacterial multidrug ATP-binding cassette transporter.
Product Overview
The trypsin molecule has two domains: one is related to the enzyme active site and the tryptophan residues; the other is related to the 8-anilinonaphthalene-1-sulfonate binding.
Enzyme Commission Number
EC 3.4.21.4
Activity
> 8,500 BAEE units/mg protein (biuret)
Unit Definition
One BAEE unit will produce a ΔA253 of 0.001 per min at pH 7.6 at 25° C using BAEE as substrate. Reaction volume = 3.2 mL (1 cm light path).
Pathway
Activation of Matrix Metalloproteinases, organism-specific biosystem; Defective GIF causes intrinsic factor deficiency, organism-specific biosystem; Defective CD320 causes methylmalonic aciduria, organism-specific biosystem
Function
calcium ion binding; serine-type endopeptidase activity
Synonyms
α-trypsin; β-trypsin; cocoonase; parenzyme; parenzymol; tryptar; trypure; pseudotrypsin; tryptase; tripcellim; sperm receptor hydrolase; Alpha-trypsin; Beta-trypsin; EC 3.4.21.4; Trypsin; Acetyltrypsin