Isolation and properties of reduced nicotinamide adenine dinucleotide phosphate-hepatoredoxin reductase of rabbit liver mitochondria. |
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Authors: | Y Ichikawa A Hiwatashi |
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Institution: | Department of Biochemistry, Osaka University Medical School 33-Joan-cho, Kita-ku, Osaka 530, Japan |
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Abstract: | An NADPH-hepatoredoxin reductase was purified from mitochondria of rabbit hepatocytes. The optical absorption spectrum showed a typical flavoprotein. The NADPH-hepatoredoxin reductase has an FAD as a coenzyme and the molecular weight of the NADPH-hepatoredoxin reductase was estimated to be 51000 by SDS-polyacrylamide gel electrophoresis. The NADPH-hepatoredoxin reductase was immunochemically similar to NADPH-adrenodoxin reductase of bovine and pig adrenocortical mitochondria, but not NADPH-cytochrome P-450 reductase of rabbit liver microsomes. The NADPH-cytochrome c reductase activity of the NADPH-hepatoredoxin reductase and hepatoredoxin complex, unlike NADPH-cytochrome P-450 reductase, was decreased by increasing ionic strength. |
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