Glutathione S-transferase, similar to sigma class, from skin secretions of Xenopus laevis.
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.
Pennelli
A
A
Dipartimento di Scienze Biomediche, Università G. D'Annunzio, Chieti, Italy.
Ortolano
S
S
Miele
R
R
Renda
T
T
Sacchetta
P
P
Di Ilio
C
C
Simmaco
M
M
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*
D007527:Isoenzymes; D005982:Glutathione Transferase