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Inhibition of bovine kidney low molecular mass phosphotyrosine protein phosphatase by uric acid

José Mauro Granjeiro Carmen Verissima Ferreira; Paulo Afonso Granjeiro; Cinthia Celestino da Silva Silva; Pedro Luiz Onofre Volpe; Hiroshi Aoyama

Journal of Enzyme Inhibition and Medicinal Chemistry v. 17, n. 5, p. 345-350, 2002

Item não circula. Consulte sua biblioteca.(Acessar)

Título:
Inhibition of bovine kidney low molecular mass phosphotyrosine protein phosphatase by uric acid
Autor: José Mauro Granjeiro
Carmen Verissima Ferreira; Paulo Afonso Granjeiro; Cinthia Celestino da Silva Silva; Pedro Luiz Onofre Volpe; Hiroshi Aoyama
Assuntos: PROTEÍNAS; ÁCIDOS; INIBIÇÃO
É parte de: Journal of Enzyme Inhibition and Medicinal Chemistry v. 17, n. 5, p. 345-350, 2002
Descrição: 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 IND. ic' and 'K IND. iu' values of 0.4 and 1.0 mM, respectively; the inhibition by uric acid shifted the pH optimum from 5.0 to 6.5. Whem Tyr-P was the substrate, competitive inhibition was observed with a 'K IND. 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 phosphated suggest that the interaction of uric acid with the enzyme occured at the active site, but did not involve SH residues, and that the mechanism of inhibition depended on the structure of the substrates
Editor: London
Data de criação/publicação: 2002
Formato: p. 345-350.
Idioma: Inglês

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