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JBC, Vol. 252, Issue 23, 8423-8427, Dec, 1977

Residual esterase activity of lima bean inhibitor-binding anhydrochymotrypsin preparations

M. S. Matta, P. A. Henderson, H. D. Drew, A. C. Wilbraham, J. G. Benitez, J. M. Mudd and D. K. North

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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