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 (NH(4))(2)SO(4) 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(-3)m. Sulfhydryl inhibitors and sodium fluoride had no effect on enzyme activity at a concentration of 10(-3)m. 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.