Rabbit kidney aminopeptidases: purification and some properties

Rabbit kidney aminopeptidases: purification and some properties

Author Oliveira, S. M. Google Scholar
Freitas, J. O. Google Scholar
Alves, K. B. Google Scholar
Institution Universidade Federal de São Paulo (UNIFESP)
Abstract Aminopeptidases (EC.3.4.11...) are widely distributed in nature and have medical and biological importance due to their function in the modification and degradation of protein. Two aminopeptidases were purified from rabbit kidney homogenate by ion exchange and gel filtration chromatography columns, using aminoacyl of beta-naphthylamides and p-nitroanilides as substrates. the enzymes' homogeneity was assured by SDS-PAGE. the first enzyme (P-1) has an optimum of pH 7.0, a molecular mass of 70 kDa, best catalytical efficiency for methionyl-beta-naphthylamide, is 70% inhibited by 0.5 mM Zn2+ and Co2+ ions, 3.33 mM sodium hydrocortisone succinate and 0.08 mM p-hydroxymercuribenzoate, and is little or not inhibited by EDTA, amino acids, p-nitroaniline, beta-naphthylamine, deoxicholate, bestatin and puromycin. the second enzyme (P-2) has an optimum of pH 7.0, a molecular mass of 54 kDa, best catalytical efficiency for Leu-beta-naphthylamide, is inhibited by 0.5 mM ions Zn2+ (45%), 0.02 mM EDTA (94%) 0.08 mM p-hydroxymercuribenzoate (70%), 3.33 mM beta-ME (13%), 1.33 mM p-nitroaniline (40%), 1.33 mM beta-naphthylamine (17%), 1.33 mM sodium deoxicholate (96%), 3.33 mM sodium hydrocortisone succinate (60%), and is 30% activated by 0.5 mM Co2+ ions. Puromycin and bestatin are competitive inhibitors with K-i values in 10(-6) and 10(-7) M order, respectively. P-1 is a methionine aminopeptidase, while P-2 is a leucine aminopeptidase. (C) 1999 Elsevier Science B.V. All rights reserved.
Keywords rabbit kidney
aminopeptidase
arylamidase
arylaminopeptidase
rabbit
Language English
Date 1999-12-01
Published in Immunopharmacology. Amsterdam: Elsevier B.V., v. 45, n. 1-3, p. 215-221, 1999.
ISSN 0162-3109 (Sherpa/Romeo, impact factor)
Publisher Elsevier B.V.
Extent 215-221
Origin http://dx.doi.org/10.1016/S0162-3109(99)00080-6
Access rights Closed access
Type Article
Web of Science ID WOS:000084080100034
URI http://repositorio.unifesp.br/handle/11600/26189

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