Electron transport systems of lung microsomes and their physiological functions. Enzymic hydroxylation of aniline and steroids.
Xenobiotica, 1975/4;5(4):205-12.
Matsubara T, Nakamura Y, Tochino Y
PMID: 239487
Impact factor: 1.997
Abstract
1. The hydroxylation of aniline by rabbit lung microsomes to rho-aminophenol required oxygen and NADPH, and was inhibited by menadione, ferricytochrome c and carbon monoxide. 2. NADH was a less effective electron donor than NADPH in this reaction, but its addition significantly increased the yield of rho-aminophenol formed in the presence of NADPH. 3. 4,16-Androstadien-3-one and 3beta-hydroxy-5-androsten-17-one were also metabolized by lung microsomes to the same products as are formed by hepatic microsomes.
MeSH terms
Androstadienes; Androstenols; Aniline Compounds; Animals; Carbon Monoxide; Cell-Free System; Chromatography, Thin Layer; Cytochrome P-450 Enzyme System; Cytochrome c Group; Electron Transport; Hydroxylation; Lung; Male; Microsomes; Microsomes, Liver; NADP; NADPH-Ferrihemoprotein Reductase; Oxygen; Phenols; Rabbits; Steroids; Subcellular Fractions; Vitamin K
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