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　CM-Sephadex　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　mu　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.