Characterization of S-hexylglutathione-binding proteins of human hepatocellular carcinoma: separation of enoyl-CoA isomerase from an Alpha class glutathione transferase form.

@article{KajiharaKano1997CharacterizationOS,
  title={Characterization of S-hexylglutathione-binding proteins of human hepatocellular carcinoma: separation of enoyl-CoA isomerase from an Alpha class glutathione transferase form.},
  author={Hiroko Kajihara-Kano and Makoto Hayakari and Kimihiko Satoh and Yoshihisa Tomioka and Michinao Mizugaki and Shigeki Tsuchida},
  journal={The Biochemical journal},
  year={1997},
  volume={328 ( Pt 2)},
  pages={473-8}
}
Recent studies have revealed binding of mitochondrial enoyl-CoA isomerase (ECI) to S-hexylglutathione-Sepharose, an affinity matrix used for purification of glutathione transferases (GSTs), and the enzyme has been suggested to be identical with the Alpha class form of GST with a subunit molecular mass of about 30 kDa. In the present study, S-hexylglutathione-binding proteins of human hepatocellular carcinomas were characterized to examine their identity. Supernatant fractions of carcinoma and… CONTINUE READING