Human brain monoamine oxidase: one molecular entity-multiple binding sites?
- 1 September 1981
- journal article
- research article
- Published by Oxford University Press (OUP) in Journal of Pharmacy and Pharmacology
- Vol. 33 (1), 165-170
- https://doi.org/10.1111/j.2042-7158.1981.tb13741.x
Abstract
Monoamine oxidase (MAO) of human brain cortex was partially characterized by using different substrates and inhibitors. Two Km values were calculated for each of the three substrates tested, i.e., phenethylamine (PEA), benzylamine (BA) and 5-hydroxtryptamine (5-HT). Clorgyline and 5-HT, both known as MAO-A occupants, were able to abolish the second (high) Km deamination of PEA. 5-HT, while non-competitively inhibiting the deamination of low BA concentrations, competitively inhibited the deamination of high concentrations of this type B substrate. The kinetics of 5-HT deamination showed positive cooperation which indicates the involvement of subunits in the enzyme structure. The ability of some phospholipids to change the enzyme behaviour was considered as indication that these molecules might play a role in determining the ratio between the so-called A and B types of MAO, and in the regulation of the enzyme's activity.This publication has 22 references indexed in Scilit:
- Oxidation of β-phenylethylamine by both types of monoamine oxidase: Effects of substrate concentration and PHLife Sciences, 1979
- Activation of platelet monoamine oxidase by plasma in the humanLife Sciences, 1979
- Multiple forms of monoamine oxidase in human brain tumorsNeuroscience Letters, 1978
- Possible heterogeneity of type B monoamine oxidase in pig heart mitochondriaBiochemical Pharmacology, 1978
- Monoamine oxidase A and B: A useful concept?Biochemical Pharmacology, 1978
- Purification and some properties of porcine brain mitochondrial monoamine oxidase BBiochemical Pharmacology, 1978
- Lysolecithin is a selective reversible inhibitor of mitochondrial monoamine oxidaseBiochemical Pharmacology, 1978
- MULTIPLE BINDING SITES OF HUMAN BRAIN AND LIVER MONOAMINE OXIDASE: SUBSTRATE SPECIFICITIES, SELECTIVE INHIBITIONS, AND ATTEMPTS TO SEPARATE ENZYME FORMSJournal of Neurochemistry, 1977
- Monoamine oxidase: Examination of multiple formsLife Sciences, 1977
- On the nature of allosteric transitions: A plausible modelJournal of Molecular Biology, 1965