Enzymic oxidation of reduced α-nicotinamide adenine dinucleotide

Hiroshi Okamoto, Arata Ichiyama, Osamu Hayaishi

研究成果: Article査読

4 被引用数 (Scopus)

抄録

Reduced α-nicotinamide adenine dinucleotide (α-NADH) is oxidized at about one fifth of the rate of reduced β-nicotinamide adenine dinucleotide by rat liver mitochondria that have been treated with a hypotonic medium. Essentially no oxidation is observed with intact mitochondria. Oxidation is almost completely inhibited by 1 mm cyanide, but is insensitive to 1 μm antimycin A, 1 μm rotenone, and 2 mm anytal. Furthermore, enzyme activities have been detected that catalyze the transfer of electrons from α-NADH to cytochrome c and to 2,6-dichlorophenolindophenol and are seemingly localized in the microsomal and soluble fractions, respectively.

本文言語English
ページ(範囲)110-114
ページ数5
ジャーナルArchives of Biochemistry and Biophysics
118
1
DOI
出版ステータスPublished - 1967 1
外部発表はい

ASJC Scopus subject areas

  • 生物理学
  • 生化学
  • 分子生物学

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