Basic aminopeptidase from rabbit kidney: Purification and partial characterization

Basic aminopeptidase from rabbit kidney: Purification and partial characterization

Author Oliveira, S. M. Google Scholar
Freitas, J. O. Google Scholar
Alves, Kaethy Bisan Autor UNIFESP Google Scholar
Institution Universidade Federal de São Paulo (UNIFESP)
Abstract The aminopeptidase activity of a homogenate of rabbit kidney treated with Triton X-100 was measured using L-aminoacyl-2-naphthylamides (AA-NA). After gradient elution ion-exchange chromatography, four peaks of aminopeptidase activity were eluted. The enzyme eluted at 450 mu S containing 33.5% of the activity towards Arg-NA was applied to a Superdex 75 column and presented only one protein band on 10% SDS-polyacrylamide gel electrophoresis. This enzyme has an apparent molecular mass of 78 kDa, is five-fold activated by 0.15 M NaCl and the highest V-max/K-M ratio was obtained with Arg-NA. Enzyme activity was inhibited 100% by 0.13 mM sodium p-hydroxymercuribenzoate, 20% by 0.75 mM EDTA and 100% by 0.66 mM o-phenanthroline. Puromycin and bestatin behaved like competitive inhibitors with a K-i of 0.60 mM and 5.0 mu M, respectively.
Keywords rabbit kidney aminopeptidase
rabbit kidney arylamidase
Language English
Date 1996-11-01
Published in Brazilian Journal Of Medical And Biological Research. Sao Paulo: Assoc Bras Divulg Cientifica, v. 29, n. 11, p. 1437-1439, 1996.
ISSN 0100-879X (Sherpa/Romeo, impact factor)
Publisher Assoc Bras Divulg Cientifica
Extent 1437-1439
Access rights Closed access
Type Article
Web of Science ID WOS:A1996VR61500004

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