Inorganic pyrophosphatase activities extracted from vegetative cells and spores ol Bacillius Imnegateriulmz 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 witlh Mn++; both forms of the enzyme required Mn++ for stabilization in solution as well as for activity. Inorganic pyrophosphatases obtained in a near homogeneous state from vegetative cells and spores of Bacillus subtilis proved to be indistinguishable when judged by a number of physical and functional criteria (H. Tono and A. Kornberg, J. Biol. Chem., in press). Similar results were obtained in recent studies of deoxyribonucleic acid (DNA) polymerase (1) and adenylate kinase in B. subtilis (J. A. Spudich and A. Kornberg, unpublished data), or nucleoside phosphorylase in B. cereius (R. Gardner and A. Kornberg, J. Biol. Chem., in press), and in studies of other enzymes as reviewed by Halvorson (2). From these results we derive the impression that a given spore enzyme and its vegetative-cell counterpart are the same despite their markedly different resistance to heat when tested in situ. For the long-range objective of defining the components and organization of a spore and the mechanisms