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PURIFICATION AND CHARACTERIZATION OF STAPHYLOCOAGULASE¹

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

ABSTRACT

ZOLLI, ZENO, JR. (Michigan State University, East Lansing), AND CHARLES L. SAN CLEMENTE. Purification and characterization of staphylocoagulase. J. Bacteriol. 86:527–535. 1963.—Separation and extreme purification of coagulase from Staphylococcus aureus strain 70 was achieved by using three cycles of dialysis in ethanol-water mixtures under controlled conditions, followed by molecular sieving through a column of Sephadex G-200. By manipulation of five variables (pH, ionic strength, temperature, protein, and ethanol concentration), the final preparation showed an approximate 3700-fold increase in activity per mg of protein. The successfully isolated coagulase containing 15.0% nitrogen was characterized serologically and chemically. By use of agar diffusion techniques, one zone of precipitation was obtained with the highly purified material. Additional confirmation of purity was evidenced by the appearance of a single peak with cellulose acetate paper electrophoresis with a barbital buffer at pH 8.6. Progressive and eventual elimination of carbohydrate, deoxyribonuclease, lipase, and phosphatase was observed through the four stages of purification. Temperature studies showed that the stability of each fraction was inversely related to its purity.

² Present address: Virus Research Division, Chas. Pfizer and Co., Inc., Terre Haute, Ind.

¹ Published with the permission of the Director of the Michigan Agricultural Experiment Station as Journal Article Number 3149. 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. degree requirements.