Abstract
A malate dehydrogenase (MDH) was identified and isolated from the seeds of the mung bean ( Phaseolus mungo ). The procedure entailed extraction, ammonium sulfate precipitation, ion exchange chromatography on CMSephadex and high performance liquid chromatography on POROS HS-20. The purified protein exhibited a molecular mass of 38 kDa in SDS-polyacrylamide gel electrophoresis under both nonreduced and reduced conditions. The pI was 9.7 by isoelectric focusing. The specific activity of the MDH was estimated to be 199 U/mg. The enzyme expressed its optimum activity at pH 7.2, 35C, and showed stable activity below 40C. The Km for oxaloacetate was 112 μ M. The partial N-terminal amino acid sequence data analysis of the first 20 amino acids of the mung bean MDH revealed 95 and 80% homology with two reported MDH from soya bean ( Glycine max ) and potato ( Solanum tuberosum ), respectively.
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