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J Bacteriol. 1962 May; 83(5): 941-947
Copyright © 1962, The Williams & Wilkins Company. All Rights Reserved.

BIOCHEMICAL STUDIES ON STAPHYLOCOAGULASE AND AN ALLIED PHOSPHATASE ACTIVITY¹

^a Department of Microbiology and Public Health, Michigan State University, East Lansing, Michigan

ABSTRACT

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 K_s 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.

² Present address: Biochemical Research Laboratory, The Dow Chemical Company, Midland, Mich.

¹ Published with the permission of the Director of the Michigan Agricultural Experiment Station as Journal Article No. 2867. Part of a dissertation submitted to the School for Advanced Graduate Studies, Michigan State University, by the senior author in partial fulfillment of the Ph.D. requirements.