INORGANIC PYROPHOSPHATASE OF DESULFOVIBRIO DESULFURICANS
AUTOR(ES)
Akagi, J. M.
RESUMO
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 Ks for the pyrophosphatase was found to be in the region of 1.9 × 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.
