Journal
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
Volume 282, Issue 5, Pages 1268-1274Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1006/bbrc.2001.4707
Keywords
glutathione; human glutathione S-transferase; 4-hydroxynonenal
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Funding
- NCI NIH HHS [CA 77495, CA 76348, CA27967, CA 55589] Funding Source: Medline
- NEI NIH HHS [EY 04396] Funding Source: Medline
- NIEHS NIH HHS [ES 07804] Funding Source: Medline
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The two previously reported human glutathione S-transferase isszymes, hGST5.8 and hGSTA4-4, hare been suggested to be similar because of their comparable activities toward 4-hydroxynonenal-GSH conjugation, Here, we demonstrate that hGST5.8 and hGSTA4-4 are distinct, Antibodies raised against hGSTA4-4 did not recognize hGST5.8, and antibodies raised against mouse GSTA4-4 that cross-react with hGST5.8 did not recognize hGSTA4-4 The pi value of hGSTA4-4 was found to be 8.4, as opposed to the pi value of 5.8 for hGST5.6. The two isozymes are differentially expressed in human tissues and there are significant differences in their kinetic properties, While both isozymes showed a strong expression in liver and testis, hGSTA4-4 was not detected in brain where EGST5.8 was present. In the pancreas, a strong expression of hGST5.8 was observed while hGSTA4-4 was barely detectable in this tissue, (C) 2001 Academir Press.
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