[A new method of preparing and some properties of high molecular weight monoamine oxidase from swine liver mitochondria].
Isolation of highly purified and highly molecular monoamine oxidase (MAO) from pig liver mitochondria have been worked out. Specific activity of isolated preparation is 2700 times higher than of original mitochondria homogenate. Enzyme solubilization by digitonin, affinity chromatography purification and ultrafiltration underlie this method. MAO catalytic properties changing during the process of purification by different methods have been investigated. Substrate specificity was studied; kinetic parameters of enzymatic desemination were calculated.
Nikol'skaia
E B
EB
Sechenov Institute of Evolutionary Physiology and Biochemistry, Russian Academy of Sciences, St. Petersburg.
Iagodina
O V
OV
Grinberg
B A
BA
Dianova
M M
MM
D000818:Animals; D002846:Chromatography, Affinity; D002850:Chromatography, Gel; D003641:Deamination; D007700:Kinetics; D008930:Mitochondria, Liver / Q000201:enzymology*; D008970:Molecular Weight; D008995:Monoamine Oxidase / Q000302:isolation & purification* / Q000378:metabolism; D013379:Substrate Specificity; D013552:Swine
D008995:Monoamine Oxidase
Novyĭ sposob polucheniia i nekotorye svoĭstva vysokomolekuliarnoĭ monoaminoksidazy iz mitokhondriĭ pecheni svin'i.