منابع مشابه
The Specificity of Carboxypeptidase
All the information hitherto available with respect to the specificity of carboxypeptidase has been obtained by the use of crude enzyme preparations (1). Consequently, there still remains some uncertainty as to whether the previously reported hydrolyses of various synthetic substrates, attributed to the action of carboxypeptidase, are all due to the same enzyme. Indeed, Abderhalden and Abderhal...
متن کاملCARBOXYPEPTIDASE B I. PURIFICATION OF THE ZYMOGEN AND SPECIFICITY OF THE ENZYME* BY J. E. FOLKt
An enzyme capable of rapidly releasing carboxyl terminal lysine and arginine has been reported as an act,ive component of autolyzed bovine pancreas (2). In the same report it was recognized that this enzyme, carboxypeptidase B or basic carboxypeptidase, exists in fresh pancreas as an inactive zymogen which is activated by t,reatment of extra&s with trypsin. Although carboxypeptidase A’ is routi...
متن کاملCarboxypeptidase B.I. Purification of the zymogen and specificity of the enzyme.
An enzyme capable of rapidly releasing carboxyl terminal lysine and arginine has been reported as an act,ive component of autolyzed bovine pancreas (2). In the same report it was recognized that this enzyme, carboxypeptidase B or basic carboxypeptidase, exists in fresh pancreas as an inactive zymogen which is activated by t,reatment of extra&s with trypsin. Although carboxypeptidase A’ is routi...
متن کاملSubstrate specificity of human metallocarboxypeptidase D: Comparison of the two active carboxypeptidase domains
Metallocarboxypeptidase D (CPD) is a membrane-bound component of the trans-Golgi network that cycles to the cell surface through exocytic and endocytic pathways. Unlike other members of the metallocarboxypeptidase family, CPD is a multicatalytic enzyme with three carboxypeptidase-like domains, although only the first two domains are predicted to be enzymatically active. To investigate the enzym...
متن کاملOn the specificity of chicken pancreas conjugase (gamma-glutamic acid carboxypeptidase).
The early studies on conjugase from chicken pancreas (1, 2) did not lead to the identification of this enzyme. Subsequent progress in the elucidation of the chemical structure of pteroylglutamic acid (3) and its derivatives (4, 5) left little doubt that conjugase is one of the peptidases. Pfiffner et al. (4) classified the conjugase enzymes as carboxypeptidases after they showed that the methyl...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1940
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(18)73265-1