Enzymic oxidation of the indole nucleus of 5-hydroxytryptamine: Properties of an enzyme in human serum and of the products of oxidation
1960; Elsevier BV; Volume: 90; Issue: 2 Linguagem: Inglês
10.1016/0003-9861(60)90569-5
ISSN1096-0384
AutoresGeorge M. Martin, Earl P. Benditt, Nils Eriksen,
Tópico(s)Electrochemical Analysis and Applications
Resumo5-Hydroxytryptamine (5-HT) consumes oxygen in the presence of pooled serum from pregnant humans and ceruloplasmin concentrates. The properties of the catalyst in serum were those of an enzyme. 5-HT oxidase may be identical with the enzyme which oxidizes p-phenylenediamine. Chromatography of incubation mixtures containing 5-HT and serum or 5-HT and ceruloplasmin concentrates revealed several indolic products as well as a pigment having properties similar to the melanins. These products appear to be identical with those resulting from 5-HT oxidation by air in the presence of copper or by AgNO3; the major product of the latter reaction has been identified as a dimer resulting from dehydrogenative coupling of the indole nuclei of two molecules of 5-HT (1).
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