Your browser doesn't support javascript.
loading
Show: 20 | 50 | 100
Results 1 - 3 de 3
Filter
Add more filters










Database
Language
Publication year range
3.
J Biol Chem ; 252(23): 8423-7, 1977 Dec 10.
Article in English | MEDLINE | ID: mdl-925002

ABSTRACT

A search for the source of the residual esterase activity of crude lima bean protease inhibitor-binding anhydrochymotrypsin preparations was undertaken. The preparations were found to contain about 40% of protein that possesses 1% (kc/Km) to 12% (kc) of the esterase activity of alpha-chymotrypsin. The active protein was isolated by affinity chromatography on soybean trypsin inhibitor-Sepharose. It appears to be an anhydroenzyme or a mixture of a limited number of anhydroenzymes in which a serine other than the catalytically essential serine-195 of the native enzyme has been converted to dehydroalanine.


Subject(s)
Chymotrypsin/metabolism , Esterases/metabolism , Plants/enzymology , Chromatography, Affinity , Chymotrypsin/isolation & purification , Esterases/isolation & purification , Kinetics , Trypsin Inhibitor, Bowman-Birk Soybean
SELECTION OF CITATIONS
SEARCH DETAIL
...