ABSTRACT
Ethoxyformic acid anhydride, amino-1-H-tetrazole, and photooxidation using Rose Bengal inactivated mitochondrial monoamine oxidases (MAO). There have been a limited number of kinetic studies conducted with highly purified bovine liver Monoamine oxidase B (MAO-B). A new type of MAO which is unlike Monoamine oxidase A (MAO-A) or MAO-B has recently been isolated from pig liver by K. Yagi and M. Naoi. The procedure used was a modification of the procedure used to purify the bovine heart MAO reported above and included several additional steps such as octyl-sepharose chromatography and crystallization. The general conclusion made was the delipidation of mitochondria or enzyme resulted in loss of MAO-A or MAO-B activity. Except for one report for a general nonspecific activation of MAO in delipidated mitochondria, various specific phospholipids were reported to reactivate one form of MAO, e.g. phosphatidyl inositol activated delipidated MAO-A activity. Crystallization of MAO is possible as Yagi and Naoi have reported for the pig liver MAO.
