| Literature DB >> 14221486 |
D Y COOPER, S LEVIN, S NARASIMHULU, O ROSENTHAL.
Abstract
The reversal of the carbon monoxide inhibition by bands of monochromatic light was determined for the oxidative demethylation of codeine and monomethyl-4-aminopyrine and the hydroxylation of acetanilide by rat liver microsomes and for the hydroxylation of 17-hydroxyprogesterone at carbon-21 by bovine adrenocortical microsomes. Maximum reversal occurred at 450 millimicrons, the light absorption maximum of the CO compound of the CO-binding pigment of microsomes. The agreement between photochemical action spectrum and spectrophotometric difference spectrum supports the conclusion that the CO-binding pigment is the terminal oxidase of mixed function oxidase systems of mammals.Entities:
Keywords: ACETANILIDE; AMINOPYRINE; CARBON MONOXIDE; CODEINE; EXPERIMENTAL LAB STUDY; HYDROXYLASES; HYDROXYPROGESTERONE; LIGHT; LIVER ENZYMOLOGY; MICROSOMES; OXYGENASES; RATS
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Year: 1965 PMID: 14221486 DOI: 10.1126/science.147.3656.400
Source DB: PubMed Journal: Science ISSN: 0036-8075 Impact factor: 47.728