CARBOXYL TERMINAL GROUPS OF PROTEOLYTIC ENZYMES
نویسندگان
چکیده
منابع مشابه
Carboxyl-terminal proteolytic processing of matrix Gla protein.
The present study was undertaken to determine the extent of COOH-terminal proteolytic processing in matrix Gla protein (MGP), a 10-kDa protein which contains 5 residues of the vitamin K-dependent Ca2+ binding amino acid, gamma-carboxyglutamic acid (Gla). Two forms of MGP were isolated from demineralization and urea extracts of bovine cortical bone, one 79 residues in length with the COOH termin...
متن کاملProteolytic modification of the amino-terminal and carboxyl-terminal regions of rat hepatic phenylalanine hydroxylase.
Activation of rat liver phenylalanine hydroxylase by limited proteolysis catalyzed by chymotrypsin was investigated with the use of sodium dodecyl sulfate-polyacrylamide gel electrophoresis and high pressure gel filtration. Both activation and proteolysis were decreased by the addition of the natural cofactor, (6R)-tetrahydrobiopterin. From chymotryptic digests of the hydroxylase carried out in...
متن کاملProteolytic enzymes.
Leipner, J. and R. Saller (2000). "Systemic enzyme therapy in oncology: effect and mode of action." Drugs 59(4): 769-80. Plant extracts with a high content of proteolytic enzymes have been used for a long time in traditional medicine. Besides proteolytic enzymes from plants, 'modern' enzyme therapy additionally includes pancreatic enzymes. The therapeutic use of proteolytic enzymes is partly ba...
متن کاملUbiquitin carboxyl-terminal hydrolase acts on ubiquitin carboxyl-terminal amides.
Ubiquitin carboxyl-terminal hydrolase (formerly known as ubiquitin carboxyl-terminal esterase), from rabbit reticulocytes, has been shown to hydrolyze thiol esters formed between the ubiquitin carboxyl terminus and small thiols (e.g. glutathione), as well as free ubiquitin adenylate (Rose, I. A., and Warms, J. V. B. (1983) Biochemistry 22, 4234-4237). We now show that this enzyme hydrolyzes ami...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1953
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(19)77260-3