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OXIDATION OF 5‐HYDROXYTRYPTAMINE AND RELATED COMPOUNDS BY MYTILUS GILL PLATES
Author(s) -
BLASCHKO H.,
MILTON A. S.
Publication year - 1960
Publication title -
british journal of pharmacology and chemotherapy
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.432
H-Index - 211
eISSN - 1476-5381
pISSN - 0366-0826
DOI - 10.1111/j.1476-5381.1960.tb01208.x
Subject(s) - mytilus , amine oxidase , byssus , iproniazid , chemistry , biochemistry , amine gas treating , serotonin , monoamine oxidase , cyanide , enzyme , biology , fishery , organic chemistry , receptor
Homogenates of gill plates of Mytilus edulis L. used oxygen when 5‐hydroxytryptamine was added. The oxidation of 5‐hydroxytryptamine was not due to the presence of an amine oxidase, but to that of an enzyme that catalysed the oxidation of other 5‐hydroxyindoles (5‐hydroxytryptophan, bufotenine). The oxidation was cyanide‐sensitive, but was not inhibited by iproniazid. In the reaction a yellowish‐brown substance was formed. The occurrence of an amine oxidase in the anterior retractor muscle of the byssus and in the digestive gland was confirmed.