English (United Kingdom)

https://curated-unify.zendy.io/wp-json/zendy-region/v1/featured_content/oa?rat=en

https://curated-unify.zendy.io/wp-json/zendy-region/v1/highlighted_journal/

Zendy Open

Presents the pdf analysis as premium feature

PDF Analysis

Insights

Presents the summarisation as premium feature

Summarisation

Presents the keyphrase highlighting as premium feature

Keyphrase Highlighting

Presents the zaia usage as premium feature

ZAIA

Zendy Tools

Zendy Plus

Presents the access of premium content as premium feature

Premium Content

On the basis of substrate specificities and inhibitor sensitivities, mitochondrial mono amine oxidase (MAO) (EC 1.4.3.4) has been classified as two forms, MAO-A and MAO-B (1). In rat liver, serotonin is preferentially oxi dized by MAO-A, which is highly sensitive to inhibition by clorgyline but less so to deprenyl (1, 2). Benzylamine and (3-phenylethylamine (PEA) are preferentially oxidized by MAO-B, and tyramine is oxidized by both forms of MAO (1, 2). However, these specificities are not always observed (3) and it has also been found that MAO-B in some tissues can oxidize serotonin to some extent (4-8). Our previous studies on rat brain MAO revealed that PEA, long regarded as a specific substrate for MAO-B, is also oxidized by MAO-A and that the ratio of MAO-A to MAO-B activity with PEA is concentration-dependent (9-13). Here, we investigated the concentration dependence of the oxidation rates of serotonin by the two forms of MAO in rat liver mito chondria. We also examined whether the oxidation with MAO-A of rat liver has a "ping -pong" or double-displacement reaction

5-Hydroxytryptamine: A substrate for rat liver mitochondrial monoamine oxidase-A and -B.