[Flavin-containing polyaminooxidase in the liver: spectral properties and localization].
Some properties of flavin-containing polyamine oxidase from bovine liver have been studied. Limited proteolysis of the enzyme by trypsin resulted in two fragments with molecular masses of 48 and 5-8 kDa. The antigenic determinants of the protein appear to be bound to the larger proteolytic fragment. The effect of proteolysis on optical properties of the enzyme has been established. Data from immunological analysis suggest that the soluble fraction of the liver is a rich source of the enzyme.
Gasparian
V K
VK
D000818:Animals; D002417:Cattle; D000939:Epitopes / Q000378:metabolism; D005415:Flavins / Q000378:metabolism*; D006868:Hydrolysis; D008099:Liver / Q000201:enzymology*; D000587:Oxidoreductases Acting on CH-NH Group Donors / Q000276:immunology / Q000378:metabolism*; D011817:Rabbits; D013050:Spectrometry, Fluorescence; D014357:Trypsin / Q000378:metabolism; D000097667:Polyamine Oxidase
D000939:Epitopes; D005415:Flavins; D000587:Oxidoreductases Acting on CH-NH Group Donors; D014357:Trypsin; D000097667:Polyamine Oxidase
Flavinsoderzhashchaia poliaminooksidaza pecheni: spektral'nye svoĭstva i lokalizatsiia.