Alfonso Pennelli1, Saida Ortolano1, Rossella Miele2, T Renda3, Paolo Sacchetta1, Carmine Di Ilio1, Maurizio Simmaco1
1Dipartimento di Scienze Biomediche, Università ‘G. D’Annunzio’, 66100 Chieti, Italy
22Dipartimento di Scienze Biochimiche “A. Rossi Fanelli”.
3Istituto di Anatomia Umana, Universit'a “La Sapienza”, Piazzale Aldo Moro 5, 00185 Rome, Italy.
Tóm tắt
AbstractUsing glutathione affinity chromatography followed by isoelectro‐focusing, 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.
