Abstract：
:The extraction and partial purification of endogenous "monoamine oxidase (MAO) inhibitor-like" material from the monkey brain are described. The endogenous material (F-1 and F-2) obtained after Bio-Gel P-2 gel filtration and silica column chromatography inhibited MAO in the monkey brain mitochondria toward 5-hydroxytryptamine (5-HT), beta-phenylethylamine (beta-PEA), tyramine and dopamine as substrates. The inhibitory effects of F-1 and F-2 were non-linear concentration dependent, and F-1 non-competitively inhibited A-form MAO, while F-2 inhibited A-form MAO competitively and inhibited B-form MAO non-competitively. These substances were more potent inhibitors of A-form than of B-form MAO. F-2 was heat stable but liable to the treatment with pepsin and trypsin. F-1 was not inactivated by heat treatment and digestion with pepsin and trypsin. F-1 may be a low molecular weight (less than 1350) compound, including certain monoamines or their metabolites or other unidentified compounds, while F-2 was a low molecular weight (about 2500) peptide.
journal_name
Biochem Pharmacoljournal_title
Biochemical pharmacologyauthors
Egashira T,Obata T,Nagai T,Kimba Y,Takano R,Yamanaka Ydoi
10.1016/0006-2952(89)90204-9subject
Has Abstractpub_date
1989-02-15 00:00:00pages
597-602issue
4eissn
0006-2952issn
1873-2968pii
0006-2952(89)90204-9journal_volume
38pub_type
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