Studies on the Purification of Staphylococcal Coagulase and Its Properties

Abstract

A purified coagulase was obtained from a culture filtrate of Staphylococcus aureus St-213 which proved to be homogenous in immunological, electrophoretical and Spinco Model E ultracentrifugal studies. Treatment of the material with trichloroacetic acid prior to passing through Dowex-1 and Diethylaminoethyl-Sephadex A-50 columns yielded a product which showed a 280 fold increase in activity per mg of nitrogen than the crude culture filtrate. The sedimentation coefficient of the treated material was S_{20, w}=1.59S.
The treated material was composed of 9 amino acids (i.e. lysin, aspartate, threonine, serine, glutamine, glycine, alanine, valine and methionine) and lacked carbohydrates, lipids and phosphates. Therefore, this purified material may be classified as a purified protein derivative (PPD) capable of exhibiting a specific coagulase type reaction against homologous and heterologous type antiserum when tested immunologically using the agar gel diffusion technique.