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Purification and characterization of the flavoenzyme glutathione reductase from rat liver.

Authors: Carlberg, I  Mannervik, B 
Citation: Carlberg I and Mannervik B, J Biol Chem. 1975 Jul 25;250(14):5475-80.
Pubmed: (View Article at PubMed) PMID:237922

Glutathione reductase from rat liver has been purified greater than 5000-fold in a yield of 20%. The molecular weights of the enzyme and its subunits were estimated to be 125,000 and 60,000, respectively, indicating that the native enzyme is a dimer. The enzyme molecular contains 2 FAD molecules, which are reducible by NADPH, GSH or dithioerythritol. The reduced flavin is instantaneously reoxidized by addition of GSSG. The steady state kinetic data are consistent with a branching reaction mechanism previously proposed for glutathione reductase from yeast (MANNERVIK, B. (1973) Biochem. Biophy. Res. Commun. 53, 1151-1158). This mechanism is also favored by the nonlinear inhibition pattern produced by NADP-+. However, at low GSSG concentrations the rate equation can be approximated by that of a simple ping pong mechanism. NADPH and the mixed disulfide of coenzyme A and GSH were about 10% as active as NADPH and GSSG, respectively, whereas some sulfenyl derivatives related to GSSG were less active as substrates. The pH activity profiles of these substrates differed from that of the NADPH-GSSG substrate pair.


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RGD Object Information
RGD ID: 1625133
Created: 2007-05-24
Species: All species
Last Modified: 2007-05-24
Status: ACTIVE


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