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. 1998 Oct;64(10):4073-5.
doi: 10.1128/AEM.64.10.4073-4075.1998.

Purification and characterization of an NAD-malic enzyme from Bradyrhizobium japonicum A1017

F Chen  1 , Y Okabe, K Osano, S Tajima
Affiliations

Purification and characterization of an NAD-malic enzyme from Bradyrhizobium japonicum A1017

F Chen et al. Appl Environ Microbiol. 1998 Oct.

Abstract

An NAD-malic enzyme was purified to homogeneity from Bradyrhizobium japonicum A1017, and its molecular characteristics were surveyed. The enzyme exhibited native and subunit molecular masses of 388 and 85 kDa, respectively, suggesting that it exists as a homotetramer, and was activated by metabolic intermediates in glycolysis. The role of the enzyme in bacteroids' carbon metabolism is discussed.

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Figures

FIG. 1
FIG. 1
SDS-PAGE of NAD-ME from B. japonicum A1017. The numbers on the left indicate molecular masses (in kilodaltons). The purified enzyme (0.5 μg) was loaded onto the gel, and protein in the gel was detected by silver staining (3).
See this image and copyright information in PMC

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