Glutathionylation by Grx1 C14S
2014.10.21

Glutathionylation can be specifically analyzed by using E. coli Grx1 C14S.

The E.coli Grx1 mutant C14S cannot reduce the disulfide in ribonucleotide reductase (RNR) in the presence of GSH, NADPH and gluathione reductase, a reaction catalyzed by E.coli Grx1. This disulfide is located in a swinging arm and easily reduced by bioth Grx1 and Trx. Nor does the mutant protein reduce disulfides in insulin. The results for RNR has been published:
Bushweller, J. H., Ňslund, F., WŁthrich, K. and Holmgren, A.: Structural and Functional Characterization of the Mutant Escherichia coli Glutaredoxin (C14-S) and Its Mixed Disulfide with Glutathione. Biochemistry, 31, 9288-9293, 1992.


GRX-04 specification 20120202.doc (doc, 39 kB)

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