Studies on the developmental expression of glutathione S-transferase isoenzymes in human heart and diaphragm.

Hirrell, Pamela A.; Hume, Robert; Fryer, Anthony A.; Collins, Mike F.; Drew, Roger; Bradwell, A.R.; Strange, Richard C.

Abstract

The developmental expression of the basic near-neutral and acidic isoenzymes of glutathione S-transferase (RX:glutathione R-transferase, EC 2.5.1.18) has been studied in heart and diaphragm. Neither these enzymes nor the putative muscle-specific GST4 isoenzyme demonstrated any developmental trends in expression. In vitro hybridisation and SDS-discontinuous polyacrylamide gel electrophoresis were used to show that the GST4 isoenzyme is a homodimer composed of monomers that have a slightly larger molecular weight than the near-neutral isoenzyme. The sensitivity of GST4 to inhibitors also appeared similar to that of the GST1 2 isoenzyme. Immunodiffusion and immunoblotting techniques were used to show that the acidic enzyme in muscle is immunologically identical to that in other tissues.

Citation

Hirrell, P. A., Hume, R., Fryer, A. A., Collins, M. F., Drew, R., Bradwell, A., & Strange, R. C. (1987). Studies on the developmental expression of glutathione S-transferase isoenzymes in human heart and diaphragm. BBA - Biochimica et Biophysica Acta, 915(3), https://doi.org/10.1016/0167-4838%2887%2990022-7

• Journal Article Type: Article
• Online Publication Date: Jan 17, 2003
• Publication Date: 1987-10
• Deposit Date: Jan 26, 2024
• Journal: Biochimica et Biophysica Acta
• Print ISSN: 0006-3002
• Publisher: Elsevier
• Peer Reviewed: Peer Reviewed
• Volume: 915
• Issue: 3
• DOI: https://doi.org/10.1016/0167-4838%2887%2990022-7
• Publisher URL: https://www.sciencedirect.com/science/article/abs/pii/0167483887900227?via%3Dihub
• PMID: 3115298