Please use this identifier to cite or link to this item: http://repositorio.unicamp.br/jspui/handle/REPOSIP/80567
Type: Artigo de periódico
Title: Inhibition of bovine kidney low molecular mass phosphotyrosine protein phosphatase by uric acid
Author: Granjeiro, JM
Ferreira, CV
Granjeiro, PA
Da Silva, CC
Taga, EM
Volpe, PLO
Aoyama, H
Abstract: Uric acid inhibited 50% of the activity of bovine kidney low molecular mass phosphotyrosine protein phosphatase at concentrations of 1.0, 0.4, 1.3, and 0.2 mM, respectively for p -nitrophenyl phosphate (p -NPP), flavine mononucleotide, beta-naphthyl phosphate and tyrosine phosphate (Tyr-P) as substrates. The mixed type inhibition of p -NPP hydrolysis was fully reversible, with K-ic and K-iu values of 0.4 and 1.1 mM, respectively; the inhibition by uric acid shifted the pH optimum from 5.0 to 6.5. When Tyr-P was the substrate, competitive inhibition was observed with a K-i value of 0.05 mM. Inhibition studies by uric acid in the presence of thiol compounds, and preincubation studies in the presence of inorganic phosphate suggest that the interaction of uric acid with the enzyme occurred at the active site, but did not involve SH residues, and that the mechanism of inhibition depended on the structure of the substrates.
Subject: low molecular mass phosphotyrosine protein phosphatase
uric acid
enzyme kinetics
inhibition
Country: Inglaterra
Editor: Taylor & Francis Ltd
Rights: fechado
Identifier DOI: 10.1080/1475636021000013939
Date Issue: 2002
Appears in Collections:Unicamp - Artigos e Outros Documentos

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