Purification and properties of biliverdin reductases from pig spleen and rat liver

Journal of Biochemistry
M NoguchiG Kikuchi

Abstract

Biliverdin reductase was purified from pig spleen soluble fraction to a purity of more than 90% as judged by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The enzyme was a monomer protein with a molecular weight of about 34,000. Its isoelectric point was at 6.1-6.2. The enzyme was strictly specific to biliverdin and no other oxiodoreductase activities could be detected in the purified enzyme preparation. The purified enzyme could utilize both NADPH and NADH as electron donors for the reduction of biliverdin. However, there were considerable differences in the kinetic properties of the NADPH-dependent and the NADH-dependent biliverdin reductase activities: Km for NADPH was below 5 microM while that for NADH was 1.5-2 mM; the pH optimum of the reaction with NADPH was 8.5 whereas that of the reaction with NADH was 6.9; Km for biliverdin in the NADPH system was 0.3 microM whereas that in the NADH system was 1-2 microM. In addition, both the NADPH-dependent and NADH-dependent activities were inhibited by excess biliverdin, but this inhibition was far more pronounced in the NADPH system than in the NADH system. IX alpha-biliverdin was the most effective substrate among the four biliverdin isomers, and the dimethylester o...Continue Reading

References

Nov 1, 1994·Preparative Biochemistry·Z Ding, Y Xu
Dec 29, 2005·Proceedings of the National Academy of Sciences of the United States of America·Yoshinori HagiwaraKeiichi Fukuyama
Apr 4, 2007·The Biochemical Journal·Edward FranklinTimothy J Mantle
Aug 4, 2010·Drug Metabolism and Disposition : the Biological Fate of Chemicals·James R ReedWayne L Backes
Jul 19, 2011·Journal of Bacteriology·Kathryn P HaleyEric P Skaar
Jan 1, 1991·Veterinary Clinical Pathology·Charles E. Cornelius
Jan 1, 1984·Critical Reviews in Toxicology·M D Maines

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Blvra
Measurement of Liver Enzyme
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