FEBS Letters | |
Reduction of protein disulfide bonds in an oxidizing environment | |
Majoul, Irina1  Söling, Hans-Dieter1  Ferrari, David1  | |
[1] Abteilung Klinische Biochemie, Universität Göttingen, Robert-Kochstr. 40, D-37070 Göttingen, Germany | |
关键词: Cholera toxin; Protein disulfide isomerase; Endoplasmic reticulum; Glutathione; Redox state; Protein disulfide; | |
DOI : 10.1016/S0014-5793(96)01447-0 | |
学科分类:生物化学/生物物理 | |
来源: John Wiley & Sons Ltd. | |
【 摘 要 】
Following retrograde transport to the endoplasmic reticulum (ER) the A-subunit of cholera toxin (CTX-A) is partially cleaved into CTX-A1 and CTX-A2 by reduction of a disulfide bridge [Majoul et al. (1996) J. Cell Biol. 133, 777–789], although the redox state in the ER favors disulfide formation. We show here that the disulfide bridge of CTX-A is cleaved in vitro already at GSH/GSSG ratios between 1 and 3. Protein disulfide isomerase (PDI) exerts only a minor accelerating effect. Various mixed disulfide intermediates (CTX-A1-S-S-CTX-A1; PDI-S-S-A2; PDI-S-S-A1) appear during CTX-A reduction. These results indicate that in the ER protein disulfide formation and protein disulfide reduction can take place simultaneously.
【 授权许可】
Unknown
【 预 览 】
Files | Size | Format | View |
---|---|---|---|
RO201912020303825ZK.pdf | 584KB | download |