Characterization of malate dehydrogenase: Electrophoresis, isoelectric focusing, thermostability, inhibition and activity studies on homogenates of various organs of Biomphalaria glabrata (mollusca: pulmonata)

Abstract

Malate dehydrogenase (MDH) from various organs of Biomphalaria glabarata shows the following characteristics under the described experimental conditions: 1. 1. MDH exists as a multiple molecular from possessing a large number of isoenzymes in each organ (from seven in columellar muscle to fourteen in the ovotestis) examined. 2. 2. Each organ MDH possesses a characteristic electrophoretic and gel-isoelectric focusing pattern. 3. 3. Many apparently similar electrophoretic bands were proved to be different by isoelectric focusing. 4. 4. The isoenzymes of each organ MDH behave differentially towards p-hydroxy mercuribenzoate and heat treatment. The MDH of the albumen gland is the most thermolabile of the MDH of all the other organs. 5. 5. Mercaptoethanol does not change the electrophoretic pattern.