Purification and characterization of the NADP-malic enzyme from Bradyrhizobium japonicum A1017.
作者信息
Chen F, Okabe Y, Osano K, Tajima S
机构信息
Department of Bioresource Science, Faculty of Agriculture, Kagawa University, Japan.
出版信息
Biosci Biotechnol Biochem. 1997 Feb;61(2):384-6. doi: 10.1271/bbb.61.384.
PMID:9058984
Abstract
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.
摘要
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