Limited Proteolysis of the Chitin - bindingand Reduction - carboxymethy ] ation of Rye Seed Chitinase - a : Role Domain in Its Chitinase Actiont
نویسنده
چکیده
By a limited proteolysis with thermolysin, rye seed chitinase-a (RSC-a) was separated into a N-terminal c}'steine-rich chitin-binding (CB-) domain (48 residues) and a cata])'tic (Cat-) domain (254 residues). The h)'drolytic activity of the isolated Cat-domain toward sotuble glycolchitin, was similar to that of RSC-a, but that toward insolub]e cot]oidal chitin was 28'M, of that of RSC-a. Five disulfide bonds in the CB-domain -'ere reduced with 2-mercaptoethano} (2-ME) in the absence of denaturing agents by an '`a]l-or-none"
منابع مشابه
Overexpression of chimeric chitinase42 enhanced antifungal activity of Trichoderma harzianum against Fusarium graminearum
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