TY - JOUR
T1 - Role of α-NADH for microsomal ethanol oxidation
AU - Okamoto, Hiroshi
PY - 1973/2/5
Y1 - 1973/2/5
N2 - α-NADH* * Reduced form of α-isomer of nicotinamide adenine dinucleotide (1, 2). was found to serve as electron donor for microsomal ethanol oxidation of rat liver. Almost no ethanol oxidation was observed with β-NADH. The α-NADH-dependent ethanol oxidation was almost completely inhibited by 0.1 mM cyanide or azide and strongly abolished in the presence of formate. α-NADH-dependent ethanol oxidation was increased by 1 mM SKF-525A, an inhibitor of microsomal mixed-function oxidase, to about 200%. These results suggested that hydrogen peroxide generated from α-NADH and molecular oxygen in microsomes might be a prerequisite step in the over-all reaction, eventually leading to the peroxidatic ethanol oxidation by catalase to acetaldehyde.
AB - α-NADH* * Reduced form of α-isomer of nicotinamide adenine dinucleotide (1, 2). was found to serve as electron donor for microsomal ethanol oxidation of rat liver. Almost no ethanol oxidation was observed with β-NADH. The α-NADH-dependent ethanol oxidation was almost completely inhibited by 0.1 mM cyanide or azide and strongly abolished in the presence of formate. α-NADH-dependent ethanol oxidation was increased by 1 mM SKF-525A, an inhibitor of microsomal mixed-function oxidase, to about 200%. These results suggested that hydrogen peroxide generated from α-NADH and molecular oxygen in microsomes might be a prerequisite step in the over-all reaction, eventually leading to the peroxidatic ethanol oxidation by catalase to acetaldehyde.
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U2 - 10.1016/0006-291X(73)91314-4
DO - 10.1016/0006-291X(73)91314-4
M3 - Article
C2 - 4347528
AN - SCOPUS:0015914565
VL - 50
SP - 793
EP - 798
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
SN - 0006-291X
IS - 3
ER -