The isozyme pattern of glutathione S‐transferases in rat heart
- 24 April 1984
- journal article
- Published by Wiley in FEBS Letters
- Vol. 169 (2), 156-160
- https://doi.org/10.1016/0014-5793(84)80309-9
Abstract
The isozyme pattern of glutathione S‐transferases of rat heart differs markedly from that of liver. Heart lacks the majority of basic isozymes recognized in rat liver, and isoelectric focusing of glutathione S‐transferases obtained from affinity chromatography on S‐hexylglutathione‐linked Sepharose 6B revealed that 3 major acidic isozymes with pI values of 6.8, 6.3 and 4.9 are present in heart, at least two of which were not found in liver. In addition, multiple bands were found in the pI range 5.0–5.5 for glutathione S‐transferase activity and protein staining.This publication has 16 references indexed in Scilit:
- Purification and characterization of a new cytosolic glutathione S-transferase (glutathione S-transferase X) from rat liverBiochemical Journal, 1983
- Tissue-specific expression of the rat glutathione S-transferases.Journal of Biological Chemistry, 1983
- Glutathione Transferases in Rat Testis.Acta Chemica Scandinavica, 1983
- A study of the structures of the YaYa and YaYc glutathione S-transferases from rat liver cytosol Evidence that the Ya monomer is responsible for lithocholate-binding activityBiochemical Journal, 1981
- [28] Glutathione transferase (human placenta)Methods in Enzymology, 1981
- Glutathione TransferasesPublished by Elsevier ,1980
- Radioimmunoassay of ligandinBiochimica et Biophysica Acta (BBA) - Protein Structure, 1977
- Glutathione peroxidase activity of glutathione-S-transferases purified from rat liverBiochemical and Biophysical Research Communications, 1977
- The Identity of Glutathione S -Transferase B with Ligandin, a Major Binding Protein of LiverProceedings of the National Academy of Sciences, 1974
- The Role of Glutathione and Glutathione S‐Transferases in Mercapturic Acid BiosynthesisAdvances In Enzymology and Related Subjects Of Biochemistry, 1969