title: Purification and immunochemical interrelationship of cytosolic and mitochondrial monoamine oxidase from rat brain.
abstract: Monoamine oxidase (MAO) was purified to homogenity from the cytosolic (105,000 g supernatant) and mitochondrial fractions of the rat brain. Antisera were raised against MAO preparations and enzyme-linked immunosorbent assay was developed for its sensitivity and immunochemical cross reactivity. The comparison of two forms of monoamine oxidase was based on a displacement ELISA, where antisera were interchanged on predetermined optimal dilutions. Both forms of the enzyme showed immunological cross reactivity. When cytosolic MAO preparation was coated and heterologous antisera were used, the cross reactivity was 36%. With mitochondrial MAO, on the other hand, heterologous antisera gave only 2.2% cross reactivity. This demonstrated that both forms of MAO possess a large number of unique antigenic determinants, thereby implying a structural difference.
authors.affiliation: Hormone and Drug Research Laboratory, School of Life Sciences, Jawaharlal Nehru University, New Delhi 110067, India.
authors.forename: M
authors.initials: M
authors.lastname: Azam
authors.forename: N Z
authors.initials: NZ
authors.lastname: Baquer