Oxidation of acetanilides to glycolanilides and oxanilic acids in rabbits.
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Acetanilides↗
Biomedical subjects
W Lenk
Publications and source records attributed to W Lenk.
[Biochemical hydroxylation of acetic acid in para-substituted acetanilides].
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Acetanilides↗
Hydroxylation of acetic acid to glycolic acid in rabbits.
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Acetanilides↗
[Metabolism of p-acetylaminopropiophenone in the rabbit].
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Acetaminophen↗
[The structure of rubromycin].
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Anti-Bacterial Agents↗
Hydroxylation of the acetamide moiety of N-arylacetamides in rabbits.
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Acetamides↗
Reaction of microsomal and cytosolic enzymes with N-arylacetohydroxamic acids.
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Aminopeptidases↗
Mixed-function oxygenation of the lower fatty acyl residues. II. The kinetics of microsomal omega- and (omega - 1)-hydroxylation of N-(4-chlorophenyl)propanamide.
Investigation of the kinetics of microsomal omega- and (omega - 1)-hydroxylation of 4,'-chloropropionanilide with rabbit liver microsomes revealed normal Michaelis-Menten behavior for that form of cytochrome P-450 which catalyzes omega-hydroxylation, and deviation from Michaelis-Menten behavior for the form(s) of the hemoprotein that catalyze(s) (omega - 1)-hydroxylation. This is deduced from linear Lineweaver-Burk plots of the kinetic data from omega-hydroxylation and from concavely curved downward plots of the kinetic data from (omega - 1)-hydroxylation. Evaluation of the apparent kinetic constants for (omega - 1)-hydroxylation was achieved by means of a computer program developed on the basis of non-linear regression analysis. The effect of inducers of microsomal oxygenases, such as phenobarbital and 3-methylcholanthrene, and of modifiers of microsomal enzyme activities, such as NADH, EDTA, nicotinamide, and SKF 525-A on the kinetics of omega- and (omega - 1)-hydroxylation has been studied. The two types of hydroxylation were affected differently, and different concentrations of the modifiers affected the hydroxylation pattern differently.
Anilides↗