title: [Properties of metlegoglobin reductase from lupine nodules].
abstract: The purification and properties of metlegoglobin reductase from lupine (Lupinus luteus L.) nodules are described. The purification procedure results in a 1056-fold purification of the enzyme with a total yield of 21%. The enzyme possesses the NADH-diaphorase activity. Metlegoglobin reductase is heterogenous during electrophoresis and isoelectric focusing. Electrophoresis produces two vicinal active bands, while isoelectrofocusing results in four active fractions. The fraction possessing the highest activity has a pI of 4.4. The enzyme is a flavoprotein, in which all flavins are represented by FAD. The molecular weight of the enzyme is 30 000. In some properties metlegoglobin reductase from lupine nodules is similar to methemoglobin reductase from erythrocytes and metmyoglobin reductase from muscles.
mesh_terms: D008058:Dihydrolipoamide Dehydrogenase / Q000302:isolation & purification / Q000378:metabolism; D005182:Flavin-Adenine Dinucleotide / Q000032:analysis; D007700:Kinetics; D007874:Leghemoglobin / Q000302:isolation & purification / Q000378:metabolism; D008970:Molecular Weight; D009247:NADH, NADPH Oxidoreductases / Q000302:isolation & purification / Q000378:metabolism*; D010944:Plants / Q000201:enzymology*
chemical_list: D007874:Leghemoglobin; D005182:Flavin-Adenine Dinucleotide; D009247:NADH, NADPH Oxidoreductases; C021793:metlegoglobin reductase; D008058:Dihydrolipoamide Dehydrogenase
vernacular_title: Metlegoglobinreduktaza kluben'kov liupina. Hekotorye svo¿istva.