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Residual esterase activity of lima bean inhibitor-binding anhydrochymotrypsin preparations.

Authors
  • Matta, M S
  • Henderson, P A
  • Drew, H D
  • Wilbraham, A C
  • Benitez, J G
  • Mudd, J M
  • North, D K
Type
Published Article
Journal
Journal of Biological Chemistry
Publisher
American Society for Biochemistry & Molecular Biology (ASBMB)
Publication Date
Dec 10, 1977
Volume
252
Issue
23
Pages
8423–8427
Identifiers
PMID: 925002
Source
Medline
Language
English
License
Unknown

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.

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