PMID: 108265May 25, 1979

Rat liver cytosolic azoreductase. Purification and characterization.

The Journal of Biological Chemistry
M T HuangA Y Lu


An azoreductase has been purified to apparent homogeneity from the hepatic 105,000 x g supernatant fraction of 3-methylcholanthrene-treated rats. In the presence of sodium dodecyl sulfate, the purified enzyme preparation electrophoreses on polyacrylamide gels as a single protein band with a molecular weight of 30,000. In the absence of detergent, chromatography of the azoreductase on Sephadex G-100 gives a molecular weight of about 52,000 suggesting that the native enzyme may exist as a dimer. The purified azoreductase has a typical flavoprotein absorption spectrum and contains 2 mol of FAD/mol of enzyme. The enzyme catalyzes the reductive fission of methyl red (2'-carboxy-4-N,N-dimethylaminoazobenzene) and a structure-activity study indicates that the 2'-carboxyl group of methyl red is essential for catalysis since other structurally related analogs are totally inactive.

Related Concepts

Azo Compounds
Cytoplasmic Matrix
p-Dimethylaminoazobenzene, (Z)-Isomer
Molecular Weight
NADH, NADPH Oxidoreductases

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