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INORGANIC PYROPHOSPHATASE OF DESULFOVIBRIO DESULFURICANS

^a Department of Microbiology, University of Illinois, Urbana, Illinois

ABSTRACT

AKAGI, J. M. (University of Illinois, Urbana) AND L. LEON CAMPBELL. Inorganic pyrophosphatase of Desulfovibrio desulfuricans. J. Bacteriol. 86:563–568. 1963.—The inorganic pyrophosphatase of Desulfovibrio desulfuricans was purified 136-fold by (NH₄)₂SO₄ and ethanol fractionation and diethylaminoethyl cellulose chromatography. Mg⁺⁺ or Mn⁺⁺ was required for optimal activity; Co⁺⁺ was only 65% as effective as Mg⁺⁺. The optimal ratio of Mg⁺⁺ to pyrophosphate was 1.0 at pH 8.0. The K_s for the pyrophosphatase was found to be in the region of 1.9 x 10^–3M. Sulfhydryl inhibitors and sodium fluoride had no effect on enzyme activity at a concentration of 10^–3M. The purified enzyme did not hydrolyze adenosine triphosphate, glycerol phosphate, diphenyl phosphate, or p-nitrophenyl phosphate. Thermal stability studies showed that the enzyme is rapidly inactivated at temperatures above 40 C.

¹ Present address: Department of Bacteriology, University of Kansas, Lawrence.