Abstract
Erythrocyte glutathione (GSH) can be rapidly depleted by incubating the cells with 1-chloro-2,4-dinitrobenzene (CDNB), which forms 2,4-dinitrophenyl-S-glutathione with GSH through the reaction catalyzed by glutathione S-transferase. GSH-CDNB conjugate thus formed stays undegraded within the erythrocytes. This indicates that in the erythrocytes, mercapturic acid pathway is inoperative. Depletion of GSH in the intact erythrocytes by CDNB results in rapid oxidation of large amounts of hemoglobin to methemoglobin. When glutathione S-transferase-free hemolysate of erythrocytes is incubated with CDNB, the depletion of GSH as well as methemoglobin formation are minimal. Glutathione peroxidase and glutathione reductase activities of the erythrocytes are not affected by CDNB. These studies provide a specific enzymatic method for rapid removal of erythrocyte GSH and also indicate that GSH is vital in maintaining a reduced environment within the erythrocytes.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 733-738 |
| Number of pages | 6 |
| Journal | Blood |
| Volume | 58 |
| Issue number | 4 |
| State | Published - 1981 |
| Externally published | Yes |
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ASJC Scopus subject areas
- Hematology
Cite this
Enzymatic conjugation of erythrocyte glutathione with 1-chloro-2,4-dinitrobenzene : The fate of glutathione conjugate in erythrocytes and the effect of glutathione depletion on hemoglobin. / Awasthi, Y. C.; Garg, H. S.; Dao, D. D.; Partridge, C. A.; Srivastava, Satish.
In: Blood, Vol. 58, No. 4, 1981, p. 733-738.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Enzymatic conjugation of erythrocyte glutathione with 1-chloro-2,4-dinitrobenzene
T2 - The fate of glutathione conjugate in erythrocytes and the effect of glutathione depletion on hemoglobin
AU - Awasthi, Y. C.
AU - Garg, H. S.
AU - Dao, D. D.
AU - Partridge, C. A.
AU - Srivastava, Satish
PY - 1981
Y1 - 1981
N2 - Erythrocyte glutathione (GSH) can be rapidly depleted by incubating the cells with 1-chloro-2,4-dinitrobenzene (CDNB), which forms 2,4-dinitrophenyl-S-glutathione with GSH through the reaction catalyzed by glutathione S-transferase. GSH-CDNB conjugate thus formed stays undegraded within the erythrocytes. This indicates that in the erythrocytes, mercapturic acid pathway is inoperative. Depletion of GSH in the intact erythrocytes by CDNB results in rapid oxidation of large amounts of hemoglobin to methemoglobin. When glutathione S-transferase-free hemolysate of erythrocytes is incubated with CDNB, the depletion of GSH as well as methemoglobin formation are minimal. Glutathione peroxidase and glutathione reductase activities of the erythrocytes are not affected by CDNB. These studies provide a specific enzymatic method for rapid removal of erythrocyte GSH and also indicate that GSH is vital in maintaining a reduced environment within the erythrocytes.
AB - Erythrocyte glutathione (GSH) can be rapidly depleted by incubating the cells with 1-chloro-2,4-dinitrobenzene (CDNB), which forms 2,4-dinitrophenyl-S-glutathione with GSH through the reaction catalyzed by glutathione S-transferase. GSH-CDNB conjugate thus formed stays undegraded within the erythrocytes. This indicates that in the erythrocytes, mercapturic acid pathway is inoperative. Depletion of GSH in the intact erythrocytes by CDNB results in rapid oxidation of large amounts of hemoglobin to methemoglobin. When glutathione S-transferase-free hemolysate of erythrocytes is incubated with CDNB, the depletion of GSH as well as methemoglobin formation are minimal. Glutathione peroxidase and glutathione reductase activities of the erythrocytes are not affected by CDNB. These studies provide a specific enzymatic method for rapid removal of erythrocyte GSH and also indicate that GSH is vital in maintaining a reduced environment within the erythrocytes.
UR - http://www.scopus.com/inward/record.url?scp=0019470706&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0019470706&partnerID=8YFLogxK
M3 - Article
VL - 58
SP - 733
EP - 738
JO - Blood
JF - Blood
SN - 0006-4971
IS - 4
ER -