COMPARISON OF THE BEHAVIOR OF CHYMOTRYPSIN AND CATHEPSIN-B TOWARDS PEPTIDYL DIAZOMETHYL KETONES

被引:60
作者
WATANABE, H
GREEN, GDJ
SHAW, E
机构
[1] Biology Department Brookhaven National Laboratory Upton
关键词
D O I
10.1016/0006-291X(79)92158-2
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Chymotrypsin is not inactivated by benzyloxycarbonyl-phenylalanyl diazomethyl ketone although disappearance of the diazo group can be followed spectroscopically. It is also inert to various dipeptide derivatives. Cathepsin B on the other hand is inactivated by this reagent, as described earlier as well as by other peptidyl diazomethyl ketones. It appears from initial studies that a phenylalanyl residue in the penultimate position of the inhibitor is favorable for effectiveness. Benzyloxycarbonyl-Phe-AlaCHN2 emerges from this work as a powerful, relatively soluble inactivator of bovine spleen cathepsin B with Ki = 1.7 × 10-6M. © 1979.
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页码:1354 / 1360
页数:7
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