Evidence that the two binding sites for trypsin on chicken ovoinhibitor are not equivalent. Dissociation of the complexes with porcine trypsin.
نویسنده
چکیده
Complexes between chicken ovoinhibitor (01) and porcine trypsin were allowed to dissociate in the presence of the active site titrant, j-nitrophenyl @‘-guanidinobenzoate, which reacts extremely rapidly with free active trypsin (T). The rate of the slower, “postburst” reaction with titrant, which is a measure of the rate of dissociation of the complexes, showed a distinct break not observed previously with bovine trypsin (ZAHNLEY, J. C., AND DAVIS, J. G. (1970) Biochemistry 9, 1428-1433). The 01-trypsin complexes dissociate according to the scheme
منابع مشابه
Preferred binding of bovine and porcine trypsins at two different sites on chicken ovoinhibitor. Reduced dissociation of mixed trypsin complexes.
Dissociation of mixed trypsin (bovine plus porcine trypsin) complexes with chicken ovoinhibitor was used to investigate the nonequivalence of the two binding sites for trypsin on the inhibitor. Previous work has shown that 1 mol of trypsin dissociates much more rapidly than the 2nd from unmixed trypsin complexes, those containing 2 mol of one kind of trypsin, bovine or porcine, per mol of inhib...
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ورودعنوان ژورنال:
- The Journal of biological chemistry
دوره 249 13 شماره
صفحات -
تاریخ انتشار 1974