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KMID : 0374919930140010079
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Inje Medical Journal
1993 Volume.14 No. 1 p.79 ~ p.88
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A Study on the Biochemical Measurements and Substrate-Related Kinetic Properties of Human Platelet Monoamine Oxidase
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Abstract
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Monoamine oxidase (MAO) is a major enzyme in the catabolism of the brain biogenic amines. Alternations in platelet MAO activity have bee reported in patients which schizophrenia, affective disroders and some other medical disorder. Platelet MAIO
was
kinetically evaluated by three different by three different assay procedures with different, substrates in 15 healthy subjects.
@ES Results were as follows.
@EN 1. Among the three assay procedures, the radioimmunoassay method using 14C Benzylaimen as a substrate was proved to be the most precise an superior than the other two, spectrofluorometry method using Kynuramine and spectrophotometry method
using
p-Benzylamine-azo-β-naphtol as a substrate.
2. Correlation sbetween Michaelis constant(Km) and maximal velosity(Vmax) values of MAO measured with radioimmunoassay using 14C-Benzylamine and spectrophotometry using p-Benzylamine-azo-β-naphtol as substrate were significant(P<.01).
3. The coefficient of variations for the two kinetic constants of platelet MAO muasured with radioimmunossay and spectrophotometry on the same day were within 10%.
Our results suggest that this simple and time-seving spectrophotometry method using Benylamine or its derivatives can be useful to study the kinetic properties of platelet MAO as equally as radioimmunossary method.
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KEYWORD
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