Reductive amination in soybean cotyledons: a survey of aminating dehydrogenases
Crude enzyme extracts from green, 11-day-old soybean (Glycine max L. var. Canadian No. 1) cotyledons were examined for aminating dehydrogenase activity. Apparent reductive amination of α-ketoisocaproate, α-ketoisovalerate, pyruvate, and β-hydroxypyruvate observed as an increase of NADH oxidation when either NH4Cl or (NH4)2SO4 was added to reaction mixtures could not be confirmed by paper cochromatography with appropriate authentic amino acids. Increase in NADH oxidation was explained by increases in activity of either non-aminating dehydrogenases or NADH oxidase caused either by a shift in pH when NH4+ was added to assay mixtures or by added Cl− and SO42−. Negative results were also obtained with glyoxylate. Reductive amination was confirmed only with α-ketoglutarate.