Isolation and characterization of an acid proteinase fromAspergillus oryzae

Autor:	M. A. Samartsev, V. I. Shitova, S. V. Kulikov, N. V. Belyakov
Rok vydání:	1981
Předmět:	chemistry.chemical_classification biology Chemistry Heat stability Peptide Plant Science General Chemistry General Biochemistry Genetics and Molecular Biology Acid proteinase Hydrolysis chemistry.chemical_compound Enzyme Biochemistry Pepsin Covalent bond biology.protein Pepstatin
Zdroj:	Chemistry of Natural Compounds. 17:288-293
ISSN:	1573-8388 0009-3130
DOI:	10.1007/bf00568521
Popis:	The heat stability, substrate specificity, and the pH optima of activation and inhibition of an acid proteinase isolated from the industrial preparation amilorizin Pkh have been studied. The enzyme has been found active in the hydrolysis of chromophoric peptide substrates of the type of Dnp-Gly-Gly-X-Arg-OH, where X = Phe, Met, Trp. Inhibition of the enzymatic activity by pepstatin and covalent inhibitors of carboxylic proteinases show that this enzyme belongs to the proteinases of the pepsin type.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_________::cf55a3b0bc1edfd18e11306773fa177c https://doi.org/10.1007/bf00568521 Zobrazit plný text záznamu Full text from SpringerLink