Abstract
Rat blood cells O-methylate noradrenaline to normetanephrine without detectable formation of norparanephrine. In contrast, a partially purified blood enzyme O-methylates the noradrenaline in both the p- and m-positions; the normetanephrine/norparanephrine ratio (12 ± 3 at pH 7.5) in the reaction products is similar to that obtained with purified rat liver catechol O-methyltransferase ( S-adenosylmethionine: catechol O-methyltransferase, EC 2.1.1.6). Incubation with whole rat blood leads to the disappearance of both normetanephrine and norparanephrine; part of the normetanephrine is demethylated to noradrenaline. The absence of p-O-methylated products when noradrenaline is incubated with whole blood can probably be accounted for by a preferential action of the degrading enzymes on norparanephrine.
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