[Purification of flavin-containing liver polyamine oxidase and luminescent properties of the ferment].
A flavin-containing polyamine oxidase was isolated in an electrophoretically homogeneous state from cattle liver cytosol. The molecular mass, subunit composition and flavin content of the enzyme were determined; flavin, was shown to be covalently bound to the protein fragment of the polyamine oxidase molecule. Some optical and luminescent properties of the native and denatured enzyme were investigated. Denaturation and quenching were found to affect the luminescent properties of polyamine oxidase.
Gasparian
V K
VK
Nalbandian
R M
RM
D000818:Animals; D002417:Cattle; D005415:Flavins / Q000032:analysis; D008099:Liver / Q000201:enzymology*; D008164:Luminescent Proteins / Q000737:chemistry / Q000302:isolation & purification*; D008970:Molecular Weight; D000587:Oxidoreductases Acting on CH-NH Group Donors / Q000737:chemistry / Q000302:isolation & purification*; D011489:Protein Denaturation / Q000502:physiology; D013053:Spectrophotometry; D000097667:Polyamine Oxidase
D005415:Flavins; D008164:Luminescent Proteins; D000587:Oxidoreductases Acting on CH-NH Group Donors; D000097667:Polyamine Oxidase
Ochistka flavinsoderzhashcheĭ poliaminooksidazy iz pecheni i liuminestsentnye svoĭstva fermenta.