[Properties of metlegoglobin reductase from lupin root nodules].

The interaction between metlegoglobin reductase from lupin root nodules cytosol and some substrates and inhibitors was studied. The Km values for electron acceptors: dichlorophenol indophenol, potassium ferricyanide, methylene blue and cytochrome c were 5.7 x 10(-5), 2.

[Properties of metlegoglobin reductase from lupine nodules].

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%.

[Metlegoglobin reductase from lupine nodules. Purification and properties].

The purification procedure and properties of metlegoglobin reductase from the soluble fraction of lupine (Lupinus luteus L.) nodules and from the proteins secreted by bacteroids Rhizobium lupini in vitro are described. The properties of both forms of enzyme were found to be similar.

[Inhibitory analysis of the respiration of bacteroids from the nodules of yellow lupine].

Oxygen uptake and reduction of C2H2 by bacteroids was found to be inhibited by low concentrations of cyanide and azide. However, oxygen uptake was not completely suppressed even by 10(-3) M KCN. Cyanide-resistant respiration was not inhibited by salicyl-hydroxamic acid, and seemed to be accomplished at the account of autoxidable flavo-proteins.