Purification and Characterization of the NADP-Malic Enzyme fromBradyrhizobium japonicumA1017 | Zendy

Fan Chen | Zendy; Youichi Okabe | Zendy; Kaoru Osano | Zendy; Shigeyuki Tajima | Zendy

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Purification and Characterization of the NADP-Malic Enzyme fromBradyrhizobium japonicumA1017

Author(s) -

Fan Chen,

Youichi Okabe,

Kaoru Osano,

Shigeyuki Tajima

Publication year - 1997

Publication title -

bioscience biotechnology and biochemistry

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 0.509

H-Index - 116

eISSN - 1347-6947

pISSN - 0916-8451

DOI - 10.1271/bbb.61.384

Subject(s) - tetramer , enzyme , dimer , malic enzyme , molecular mass , chemistry , biochemistry , bradyrhizobium japonicum , protein subunit , chromatography , biology , dehydrogenase , rhizobiaceae , bacteria , organic chemistry , gene , symbiosis , genetics

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.

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