[Transformation of mitochondrial monoaminoxidases types A and B].

Chlorgyline, a selective monoamine oxidase (MAO) of the A type inhibitor, contrary to deprenil--MAO of the B type inhibitor, prevented the appearance in the rat liver mitochondrial membrane fragments incubated under aerobic conditions of qualitatively new properties to deaminate histamine or AMP. Apparently the MAO of A type but not of B type underwent a qualitative alteration (transformation) of catalytic properties under conditions favourable for partial oxidation of SH-groups.