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2.
J Biol Chem ; 252(23): 8423-7, 1977 Dec 10.
Artículo en Inglés | MEDLINE | ID: mdl-925002

RESUMEN

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.


Asunto(s)
Quimotripsina/metabolismo , Esterasas/metabolismo , Plantas/enzimología , Cromatografía de Afinidad , Quimotripsina/aislamiento & purificación , Esterasas/aislamiento & purificación , Cinética , Inhibidor de la Tripsina de Soja de Bowman-Birk
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