Abstract
It was reported that NAD dependent malate dehydrogenase (MDH) from crude extracts of Bacillus subtilis, as well as the crystalized enzyme, showed a single band of activity in polyacrylamide gel electrophoresis (Yoshida, 1965). Murphey et al. (1967) and Murphey & Kaplan (1967) have found the same homogeneity of MDH activity in starch gel electrophoresis, but they have reported a heterogeneity of the subunits isolated from MDH tetrametric molecules with respect to their molecular weights. The present report illustrates the followings: i) MDH in crude extracts from Bacillus subtilis exhibits two isozymes which are different with respect to electrophoretic running, substrate afinity and sensitivity to heat treatment and to 4-chloromercuri benzoate. ii) The existence of two MDH isozymes in Bacillus subtilis, appears to account for the unexplained heterogeneity of the MDH subunits.
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