CAS Number 9002-07-7
EC Number 232-650-8
Enzyme Commission (EC) Number 3.4.21.4 ( BRENDA | IUBMB )
MDL number MFCD00082094
Analysis Note
One BTEE unit = 320 ATEE units
General description
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.
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).
Application
Trypsin can be used to release adherent cells from tissue culture plates for passaging. Trypsin has been used in a study to characterize ubiquitination sites by peptide based immunoaffinity enrichment. 1 Trypsin has also been used in a study to investigate the generation of antimicrobial peptides with potential for oral administration. 2
Trypsin is a serine protease used to hydrolyze proteins. Trypsin from bovine pancreas has a molecular weight of 23.8 kDa. Trypsins are used for the re-suspension of cells during cell culture and in proteomics research for the digestion of various proteins 3.
Biochem/physiol Actions
Trypsin cleaves peptide chains, amides and esters mainly at the carboxyl side of the amino acids lysine or arginine. Trypsin originates in the pancreas in the form of the zymogen trypsinogen3.