My memorial first original paper

Comp Biochem Physiol C. 1984;78(1):117-22.

Some properties of monoamine oxidase in carp heart.

Yamamoto M, Kobayashi S, Oguchi K.

Department of Pharmacology, School of Medicine, Showa University, Shinagawaku, Tokyo 142, Japan

Received 2 September 1983.

Abstract

1. Studies using clorgyline, deprenyl and semicarbazide as inhibitors showed that carp heart homogenate contained a new type of monoamine oxidase (MAO) and a clorgyline- and deprenyl-resistant amine oxidase (CRAO).

2. The deamination of monoamines by carp heart MAO proceeded in two steps by a double- displacement (ping-pong) mechanism.

3. The K_m values of the MAO for oxygen (K₀ values) with tyramine, 5-hydroxytryptamine (5-HT) and small beta, Greek -phenylethylamine (PEA) as substrates were identical (59 small mu, Greek M).

Studies using clorgyline, deprenyl and semicarbazide as inhibitors showed that carp heart homogenate contained a new type of monoamine oxidase (MAO) and a clorgyline- and deprenyl-resistant amine oxidase (CRAO). The deamination of monoamines by carp heart MAO proceeded in two steps by a double-displacement (ping-pong) mechanism. The Km values of the MAO for oxygen (K0 values) with tyramine, 5-hydroxytryptamine (5-HT) and beta-phenylethylamine (PEA) as substrates were identical (59 microM).

PMID: 6146456 [PubMed - indexed for MEDLINE]