Glutathionylation by Grx1 C14S

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)


New kit for high sensitivity GSH measurements

Measuring GSH in plasma and serum requires high sensitivity and is complicated by oxidation in samples upon storage. IMCO has developed a new kit for high sensitivity fluorescent determinations of GSH, GSSG and glutathionylated products.


Mammalian thioredoxin reductases: TR-03 and TR-03B

Mammalian thioredoxin reductase 1 (TrxR) contain an essential seleocycteine residue encoded by the stop codon UGA. This makes recombinant expression in E.coli a challenge. IMCO now has preparations of rat TrxR with unsurpassed specific activity.