title: Glutathione S-transferase, similar to sigma class, from skin secretions of Xenopus laevis.
abstract: 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.
authors.affiliation: Dipartimento di Scienze Biomediche, Università G. D'Annunzio, Chieti, Italy.
authors.forename: A
authors.initials: A
authors.lastname: Pennelli
authors.forename: S
authors.initials: S
authors.lastname: Ortolano
authors.forename: R
authors.initials: R
authors.lastname: Miele
authors.forename: T
authors.initials: T
authors.lastname: Renda
authors.forename: P
authors.initials: P
authors.lastname: Sacchetta
authors.forename: C
authors.initials: C
authors.lastname: Di Ilio
authors.forename: M
authors.initials: M
authors.lastname: Simmaco
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D005982:Glutathione Transferase / Q000737:chemistry / Q000145:classification / Q000235:genetics / Q000378:metabolism*; D007150:Immunohistochemistry; D007526:Isoelectric Point; D007527:Isoenzymes / Q000737:chemistry / Q000145:classification / Q000235:genetics / Q000378:metabolism; D008969:Molecular Sequence Data; D008970:Molecular Weight; D012867:Skin / Q000166:cytology / Q000201:enzymology*; D014982:Xenopus laevis / Q000033:anatomy & histology / Q000502:physiology*
chemical_list: D007527:Isoenzymes; D005982:Glutathione Transferase