An Ihproved Purification Method for Cytosolic Malate Dehydrogenase from Several Sources

A new purification method for cytosolic ma late dehydrogenases from several sources has been developed. The procedure, employing chromatographies on 5′AMP-Sepharose, DEAE-Sephacel and Blue-Sepharose, allows for a rapid isolation of the enzyme (% 40 hours), in large quantities, with good yields (45–54 %). The specific activity of final preparations were around 1300 I. U. /mg and were judged homogeneous by polyacrylamide gradient gel and sodium dodecyl sulfate polyacrylamide gel electrophoresis, high performance size exclusion chromatography and isoelectric focusing.