title: N-succinyl-alanyl-methionyl-S-benzylcysteine p-nitroanilide as a sensitive substrate for assaying activity of cysteine proteinases.
abstract: N-Succinyl-alanyl-methionyl-S-benzylcysteine p-nitroanilide has been found to be a very sensitive chromogenic substrate for the assay of cysteine proteinase papain, ficin and bromelain. N-Succinyl-alanyl-S-benzylcysteine p-nitroanilide and N-succinyl-alanyl-alanyl-S-benzylcysteine p-nitroanilide are also suitable for this purpose. These substrates were hydrolyzed only very slightly or not hydrolyzed at all by trypsin.
authors.affiliation: Department of Physiology, University of Agriculture, Prague, Czechoslovakia.
authors.forename: L
authors.initials: L
authors.lastname: Fukal
authors.forename: E
authors.initials: E
authors.lastname: Kasafírek
mesh_terms: D002863:Chromogenic Compounds; D003546:Cysteine Endopeptidases / Q000378:metabolism*; D007700:Kinetics; D009842:Oligopeptides; D013053:Spectrophotometry / Q000379:methods; D013379:Substrate Specificity
chemical_list: D002863:Chromogenic Compounds; D009842:Oligopeptides; C058609:N-succinyl-alanyl-methionyl-S-benzylcysteine-4-nitroanilide; D003546:Cysteine Endopeptidases