Glutathione S‐Transferase, Similar to Sigma Class, from Skin Secretions of Xenopus laevis

Abstract

SummaryUsing glutathione af nity chromatography followed by isoelectrofocusing, we puri ed 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 D 2 synthase activity. Immunohistochemistry analysis revealed that the isoenzyme was located in the cytoplasm of granular gland cells.