Authors: Saraswathi S
, Keyes MH
Semisynthetic "acid-esterase": Conformational modification of ribonuclease.
Publication date: 1984
Journal: Enzyme and Microbial Technology
Alternative URL: http://www.sciencedirect.com/science/article/B6TG1-47DM4K9-MF/2/8cb15a454ad8a892ff4caf18fafae8b4
Abstract: Bovine pancreatic ribonuclease has been modified by exposure to acidic conditions, addition of indole propionic acid and crosslinking with glutaraldehyde. The "acid-esterase" generated was purified up to 100-fold by ammonium sulphate fractionation and gel filtration on Biogel P-30. The partially purified acid-esterase hydrolysed tryptophan ethyl ester (TrEE) and N-benzoyl-L-arginine ethyl ester (BAEE) effectively at pH 6.0-6.3, but it had very little activity towards glycine ethyl ester and lysine ethyl ester. Hydrolysis of TrEE was competitively inhibited by tryptophan. The acid-esterase exhibited amidase activity towards benzoyl-L-arginine p-nitroanilide
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