Moskvitina T A, Kamyshanskaia N S, Smirnov A V, Prilipko L L, Gorkin V Z
Biull Eksp Biol Med. 1985 Jun;99(6):671-2.
The content of SH-groups and substrate specificity have been studied in purified preparations of monoamine oxidase (MAO) from human brain. It has been shown that both in schizophrenic and mentally normal persons MAO occurs in a partially oxidized state. The enzyme contains 2 SH-groups per 10(5) daltons of protein and deaminates MAO substrates (serotonin, beta-phenylethylamine) along with histamine, diamine oxidase substrate. Reduction of the partially oxidized SH-groups of MAO in schizophrenics up to 15 SH-groups per 10(5) daltons of protein (the normal value for human brain MAO) does not eliminate the histamine deaminase activity as is the case in experiments with MAO from the normal brain but, on the contrary, considerably potentiates it. The data suggest certain structural alteration of MAO in schizophrenia.
