Click here to close Hello! We notice that you are using Internet Explorer, which is not supported by Xenbase and may cause the site to display incorrectly. We suggest using a current version of Chrome, FireFox, or Safari.
XB-ART-9751
IUBMB Life 2000 Sep 01;503:203-7.
Show Gene links Show Anatomy links

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 .


???displayArticle.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.

???displayArticle.pubmedLink??? 11142348
???displayArticle.link??? IUBMB Life