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Clinical Chemistry 30: 24-27, 1984;
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Clinical Chemistry, Vol 30, 24-27, Copyright © 1984 by American Association for Clinical Chemistry

Kinetics of enzymatic O-methylation: its value in assays for catecholamines in plasma

L Mason and C Weinkove

The kinetics of enzymatic O-methylation of catecholamines were studied under conditions like those used in the radioenzymatic assay of plasma catecholamines. Inappropriate Michaelis-Menten kinetics and linear approximations of exponential equations were not used. Mathematical analysis indicated the importance of the ratio of methyl donor (S- adenosylmethionine) to substrate (catecholamine) concentration. If the reaction is incomplete, only a large ratio will allow linear approximations between product formed and initial catecholamine concentration. The use of high-concentration internal standards to correct for plasma interference may give erroneous results by reducing this ratio. Accuracy will be improved by ensuring (a) that S- adenosylmethionine is always greatly in excess of catecholamine, (b) that concentrations of added standards are of the same order as for endogenous catecholamine, and (c) that a high activity of enzyme is used, to allow the reaction to reach completion even in the presence of some inhibition.




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Copyright © 1984 by the American Association for Clinical Chemistry.