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Glutathione S-transferase, similar to sigma class, from skin secretions of Xenopus laevis

Pennelli, A ; Ortolano, S ; Miele, R ; Renda, T ; Sacchetta, P ; Di Ilio, C ; Simmaco, M

IUBMB life, September 2000, Vol.50(3), pp.203-7 [Periódico revisado por pares]

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  • Título:
    Glutathione S-transferase, similar to sigma class, from skin secretions of Xenopus laevis
  • Autor: Pennelli, A ; Ortolano, S ; Miele, R ; Renda, T ; Sacchetta, P ; Di Ilio, C ; Simmaco, M
  • Assuntos: Glutathione Transferase -- Metabolism ; Skin -- Enzymology ; Xenopus Laevis -- Physiology
  • É parte de: IUBMB life, September 2000, Vol.50(3), pp.203-7
  • Descrição: Using glutathione affinity chromatography followed by isoelectrofocusing, we purified from the skin secretion of Xenopus laevis an isoenzyme of glutathione S-transferase with an apparent subunit molecular mass of 22.5 kDa and an isoelectric point at pH 5.1. Its N-terminal amino acid sequence was highly similar to that of the sigma class glutathione S-transferase, which previously was demonstrated to have a glutathione-dependent prostaglandin D2 synthase activity. Immunohistochemistry analysis revealed that the isoenzyme was located in the cytoplasm of granular gland cells.
  • Idioma: Inglês

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