Defect in the properties of brain mitochondrial monoamine oxidase in schizophrenia

Moskvitina T.A., Kamyshanskaia N.S., Gorkin V.Z.
PubMed Id: 3953020
Year: 1986  Volume: 32  Issue: 1  Pages: 98-102
A highly purified individual form of monoamine oxidase (MAO-11b) has been isolated by means of affinity chromatography on AH-Sepharose 4B after solubilization of biomembranes from schizophrenic or normal brain tissues. The enzyme preparations obtained catalyzed deamination (both in schizophrenia and normal state) not only of serotonin and 2-phenylethylamine but also of histamine and contained about 2 SH-groups per 10(5) dalton of protein which is characteristic for "transformed" MAO with partially oxidized SH-groups. Preincubation of MAO-11b from normal brain with 10 mM dithiothreitol caused "re-transformation" of MAO: there was a marked decrease in histamine deaminating activity with simultaneous increase in the MAO activity and in content of SH-groups. In schizophrenia the re-transformation of MAO was impaired: preincubation of MAO-11b under the same conditions led to an increase in content of SH-groups and in MAO activity but the preincubation with a reducing agent did not decrease (causing, to the contrary, a marked increase) the deamination of histamine.
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Moskvitina, T. A., Kamyshanskaia, N. S., Gorkin, V. Z. (1986). Defect in the properties of brain mitochondrial monoamine oxidase in schizophrenia. Voprosy Meditsinskoi Khimii, 32(1), 98-102.
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