Cationic glutathione S-transferase of human erythrocytes has unique kinetic characteristics among human glutathione S-transferases
- 1 June 1986
- journal article
- research article
- Published by Elsevier in Biochemical and Biophysical Research Communications
- Vol. 137 (3) , 1174-1180
- https://doi.org/10.1016/0006-291x(86)90349-9
Abstract
No abstract availableThis publication has 16 references indexed in Scilit:
- Different forms of human liver glutathione s-transferases arise from dimeric combinations of at least four immunologically and functionally distinct subunitsBiochemical Journal, 1985
- Identification of a basic hybrid glutathione S-transferase from human liver. Glutathione S-transferase δ is composed of two distinct subunits (B1 and B2)Biochemical Journal, 1985
- Characterization of glutathione S-transferases of human corneaExperimental Eye Research, 1985
- Glutathione S-transferases of human brain. Evidence for two immunologically distinct types of 26500-Mr subunitsBiochemical Journal, 1985
- Glutathione S-transferases of lung: purification and characterization of human lung glutathione S-transferasesLung, 1984
- Purification and characterization of glutathione S-transferases in human retinaCurrent Eye Research, 1984
- Molecular and catalytic properties of glutathione transferase .mu. from human liver: an enzyme efficiently conjugating epoxidesBiochemistry, 1983
- Interrelationship between anionic and cationic forms of glutathione S-transferases of human liverBiochemical Journal, 1980
- Glutathione transferase from human erythrocytesArchives of Biochemistry and Biophysics, 1978
- Multiple Forms of Human Glutathione S‐Transferase and Their Affinity for BilirubinEuropean Journal of Biochemistry, 1975