Coagulase of Myxococcus fulvus NK 35. 1. Purification and partial characterization

Abstract

Summary Myxocoagulase, produced by Myxococcus fulvus NK 35 in Noren's modified medium at 30 °C in 8d, was precipitated from the cell-free filtrate by 80 % saturation with ammonium sulphate, followed by dialysis against water. It was further concentrated by polyethyleneglycol 6000. Complete purification was achieved by passing through a DEAE cellulose column, giving a single peak with 0.05M phosphate buffer, p H 7.2, containing 0.05M NaCl. The purity of the enzyme was confirmed by agar gel, Polyacrylamide gel and Immunoelectrophoresis.The pure enzyme showed a specific activity of 110,702 coagulase units/mg protein against rabbit plasma. On the basis of relative mobility in Polyacrylamide gel electrophoresis, its molecular weight was calculated as approximately 57,000 daltons. Immunological studies have shown it to be antigenically distinct from staphylocoagulase.