Isoelectric focusing of isoenzymes of monkey brain monoamine oxidase.
The multiple forms of monoamine oxidase (MAO) in monkey brain were investigated using an electrofocusing technique. When beta-phenylethylamine (beta-PEA) was used as substrate, two peaks (peak I and peak II) could be clearly distinguished from the profile; the isoelectric point (pI) values were near 7.8 and 6.3, respectively. When serotonin (5-HT) was used, MAO activity was observed in peak I enzyme. The peak I enzyme with a pI value of 7.8 contains AB-form MAO and oxidizes 5-HT and beta-PEA, while peak II enzyme with a pI value of 6.3 contains B-form MAO and oxidizes beta-PEA, respectively. However, when peak II enzyme was incubated in a pH 8.8 reaction medium, MAO activity toward 5-HT in peak II enzyme was seen.
D000818:Animals; D001921:Brain / Q000201:enzymology*; D003010:Clorgyline; D000882:Haplorhini; D006863:Hydrogen-Ion Concentration; D007525:Isoelectric Focusing; D007527:Isoenzymes / Q000302:isolation & purification*; D008995:Monoamine Oxidase / Q000302:isolation & purification*; D012642:Selegiline
D007527:Isoenzymes; D012642:Selegiline; D008995:Monoamine Oxidase; D003010:Clorgyline