Abstract
Inorganic pyrophosphatase activities extracted from vegetative cells and spores of Bacillus megaterium were compared and found to be similar in behavior on polyacrylamide gel electrophoresis, in metal and pH requirements for activity, and in response to inhibitors. In the sporulating cell, an additional electrophoretic species of the enzyme was observed which could be partially converted to the principal form by treatment with Mn++; both forms of the enzyme required Mn++ for stabilization in solution as well as for activity.
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