Abstract
An endogenous monoamine oxidase (MAO) inhibitory modulator and cytosolic MAO coexisting in the rat liver cytosol were fractionated by gel filtration following ultracentrifugation. High molecular weight fractions exhibiting MAO activity were further purified by countercurrent chromatography (CCC). MAO activity, detected using beta-phenylethylamine (β-PEA) and 5-hydroxytryptamine (5-HT) as substrates, was eluted in two separate peaks (fractions M-1, M-2) from the CCC column. Both the M-1 and M-2 fractions displayed high enzymatic activities on β-PEA whereas the M-2 fraction showed a very low MAO activity on 5-HT. This result might indicate a lack of type A MAO in the M-2 fraction due to the selective separation of endogenous MAO inhibitor. We may conclude that “endogenous MAO modulator” is present in rat liver cytosol.
Sign-in/Register to access full text options 
Free) 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a call
