Microheterogeneity of lentil seedling (Lens culinaris) amine oxidase.
Purified lentil seedling amino oxidase (LSAO) is homogeneous in the analytical ultracentrifuge, but shows heterogeneity in gel-filtration HPLC and in PAGE. Two components were obtained from HPLC and PAGE, but at least 6-7 subforms were seen by electrofocusing techniques. The chromatographic and electrophoretic forms are not interconvertible, indicating the presence of covalent differences. The electrophoretic pattern, but not the chromatographic pattern, is modified by treating the enzyme with a pool of glycohydrolases. The copper-free enzyme shows the same type of heterogeneity as the native enzyme, this ruling out the possibility that some subforms were due to the presence of apoenzyme.
D006631:Amine Oxidase (Copper-Containing); D002851:Chromatography, High Pressure Liquid; D004591:Electrophoresis, Polyacrylamide Gel; D007887:Fabaceae / Q000201:enzymology*; D000587:Oxidoreductases Acting on CH-NH Group Donors / Q000032:analysis*; D010946:Plants, Medicinal; D012639:Seeds / Q000201:enzymology
D006631:Amine Oxidase (Copper-Containing); D000587:Oxidoreductases Acting on CH-NH Group Donors