BIOCHEMICAL STUDIES ON STAPHYLOCOAGULASE AND AN ALLIED PHOSPHATASE ACTIVITY1

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Inniss, William E. (Michigan State University, East Lansing) and Charles L. SanClemente. Biochemical studies on staphylocoagulase and an allied phosphatase activity. J. Bacteriol. 83:941–947. 1962.—The present investigation was undertaken to determine whether the reported correlation between the coagulase and phosphatase activity of the staphylococci was functional. Staphylococcus aureus, phage-propagating strain 70, grown in brain heart infusion was the source of the purified coagulase. The concomitant phosphatase activity, measured spectrophotometrically at 400 mμ using p-nitrophenylphosphate as substrate, showed a parallel decrease during thermal inactivation at 37 and 56 C. Anion-exchange chromatography and electrophoresis using starch, starch gel, and paper as stabilizing media failed to separate the two activities. Since iodoacetate, ethylenediamine-tetraacetate, fluoride, azide, and p-chloromercuribenzoate always exerted different degrees of inactivation, apparently the same mechanism was not involved. This supposition was supported by subsequent saturation of the phosphatase with excess substrate (100-fold Ks value) and the demonstration that under this condition coagulase was not inhibited. During this purification process, comparable increases in specific activity occurred for both coagulase and phosphatase, indicating the presence of a common protein carrier.

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