Inhibition Patterns of Monoamine Oxidase Isoenzymes: Clinical Implications

Sandler, M.; Collins, G. G. S.; Youdim, M. B. H.

doi:10.1007/978-1-349-01085-1_1

M. Sandler³,
G. G. S. Collins³ &
M. B. H. Youdim³

Part of the book series: Biological Council ((BCSDA))

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Abstract

Monoamine oxidase (EC 1.4.3.4; MAO) is an insoluble enzyme which is widespread in the body (for review, see Blaschko, 1952). Particularly high concentrations are present in the brain, liver and salivary glands. Within the cell, the enzyme is located predominantly in mitochondria, probably in the outer membrane (Schnaitman et al., 1967), although activity has been detected in the microsomal fraction of certain organs (de Champlain et al., 1969). MAO catalyses the oxidative deamination to an aldehyde of a number of physiologically occurring monoamines, including the catecholamines and 5-hydroxytryptamine.

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Bernhard Baron Memorial Research Laboratories & Institute of Obstetrics & Gynaecology, Queen Charlotte’s Maternity Hospital, London, UK
M. Sandler, G. G. S. Collins & M. B. H. Youdim

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M. Sandler
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G. G. S. Collins
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M. B. H. Youdim
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Biochemical Mechanisms Section, Toxicology Research Unit, M.R.C. Laboratories, Carshalton, Surrey, UK
W. N. Aldridge

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Sandler, M., Collins, G.G.S., Youdim, M.B.H. (1971). Inhibition Patterns of Monoamine Oxidase Isoenzymes: Clinical Implications. In: Aldridge, W.N. (eds) A Symposium on Mechanisms of Toxicity. Biological Council. Palgrave, London. https://doi.org/10.1007/978-1-349-01085-1_1

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DOI: https://doi.org/10.1007/978-1-349-01085-1_1
Publisher Name: Palgrave, London
Print ISBN: 978-1-349-01087-5
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