Author |
Oliveira, S. M.
![]() Freitas, J. O. ![]() Alves, Kaethy Bisan ![]() ![]() |
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 |
URI | http://repositorio.unifesp.br/11600/43097 |
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