TY - JOUR
T1 - Enzymic oxidation of reduced α-nicotinamide adenine dinucleotide
AU - Okamoto, Hiroshi
AU - Ichiyama, Arata
AU - Hayaishi, Osamu
N1 - Funding Information:
1 This investigation was supported in part by research grants from the National Institutes of Health (CA-04222 and AM-10333), the Jane Coffin Childs Memorial Fund for Medical Research, the Squibb Institute of Medical Research, and the Scientific Research Fund of the Ministry of Education of Japan.
PY - 1967/1
Y1 - 1967/1
N2 - 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.
AB - 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.
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U2 - 10.1016/0003-9861(67)90284-6
DO - 10.1016/0003-9861(67)90284-6
M3 - Article
AN - SCOPUS:49949135550
VL - 118
SP - 110
EP - 114
JO - Archives of Biochemistry and Biophysics
JF - Archives of Biochemistry and Biophysics
SN - 0003-9861
IS - 1
ER -