Abstract
Glutathione S-transferases (EC 2.5.1.18) may play an important role in the detoxication of xenobiotics by catalysing their conjugation to glutathione (GSH), and also by binding them covalently and non-covalently. Multiple forms of GSH S-transferase (GST) have been demonstrated in human liver, and lung, brain, ocular tissues, and fetal fibroblasts. In the present communication we report the isoenzyme pattern of human heart GST. Human heart has one cationic (pI 8.3) and one anionic (pI 4.9) form of GST. Both these isoenzymes have been purified to homogeneity and their kinetic, structural, and immunological properties have been reported.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 973-974 |
| Number of pages | 2 |
| Journal | IRCS Medical Science |
| Volume | 13 |
| Issue number | 10 |
| State | Published - 1985 |
ASJC Scopus subject areas
- Biochemistry, Genetics and Molecular Biology(all)