Purification and Characterization of the NADP-Malic Enzyme fromBradyrhizobium japonicumA1017
Copyright policy )Purification and Characterization of the NADP-Malic Enzyme fromBradyrhizobium japonicumA1017
An NADP-malic enzyme [EC 1.1.1.40] was purified to homogeneity from Bradyrhizobium japonicum A1017, and the molecular and physiological characteristics were surveyed. The molecular mass of one subunit of the purified enzyme was evaluated to be 77,600 Da by SDS-PAGE, and the native enzyme was a tetramer in pH 7.0 and dimer in pH 8.0 conditions, showing complex oligomeric characteristics corresponding to pH value.
- Kagawa University Japan
symbiotic nitrogen fixation, Bradyrhizobium japonicum, Molecular Sequence Data, Hydrogen-Ion Concentration, NAD, malic enzyme, Bacterial Proteins, Malate Dehydrogenase, Rhizobiaceae, Amino Acid Sequence, NADP
symbiotic nitrogen fixation, Bradyrhizobium japonicum, Molecular Sequence Data, Hydrogen-Ion Concentration, NAD, malic enzyme, Bacterial Proteins, Malate Dehydrogenase, Rhizobiaceae, Amino Acid Sequence, NADP
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