Please use this identifier to cite or link to this item: http://repositorio.unicamp.br/jspui/handle/REPOSIP/60968
Type: Artigo de periódico
Title: Kinetic characterization of bovine lung low-molecular-weight protein tyrosine phosphatase
Author: Buzalaf, MAR
Taga, EM
Granjeiro, JM
Ferreira, CV
Lourencao, VA
Ortega, MM
Poletto, DW
Aoyama, H
Abstract: Protein tyrosine phosphatase is an important Glass of enzymes that plays an essential role in the cellular proliferation, differentiation, and oncogenesis. In this paper we report characterization of a low-molecular-weight protein tyrosine phosphatase purified from bovine lung. The enzyme activity was essentially independent of metal ions and sensitive to sulfhydryl reagents. Both vanadate and inorganic phosphate are competitive inhibitors, with Ki values of 0.38 mu M and 0.28 mM, respectively. Besides p-nitrophenyl phosphate, the enzyme was also able to efficiently hydrolyze tyrosine phosphate, beta-naphthyl phosphate, and flavine mononucleotide.
Subject: bovine lung
kinetics
protein tyrosine phosphatase
Country: EUA
Editor: Hemisphere Publ Corp
Rights: fechado
Date Issue: 1998
Appears in Collections:Unicamp - Artigos e Outros Documentos

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