Abstract

A. U. Wurochekke*, A. J. Nok, H. M. Inuwa and C. E. Gimba

Malate dehydrogenase was isolated and partially purified from blood stream TRYPANOSOMA VIVAX. The enzyme exists in isoenzyme forms (MDH1 and MDH2). The relative molecular weights of MDH1 and MDH2 determined by Sodium dodecyl sulphate polyacrylamide gel electrophoresis were 61 and 63 kdal. respectively. MDH2 lost activity immediately after purification. It has purification fold of 15 and percentage recovery of 31%. Similarly, MDH1 was purified 21 fold from the crude with 54% recovery. This isoenzyme was considerably stable. There was no MDH activity when the live parasites were incubated with the assay medium suggesting that the enzyme was not secreted by parasites. However, addition of detergent led to a surge in MDH activity suggesting that the enzyme is membrane bound. Malate dehydrogenase from the infective form of T. VIVAX has a stable and non – stable isoforms.