Characterization of coagulase from Staphylococcus intermedius.

A protein coagulase was isolated from Staphylococcus intermedius 6131 using bovine prothrombin-Sepharose 4B and Bio-gel P-4 column chromatographies. Homogeneity was demonstrated by the formation of a single band in polyacrylamide gel electrophoresis and isoelectric focusing. The purified preparation possesses a molecular weight of 64,500, an isoelectric point of 4.1, consists of 615 total amino acid residues and demonstrates coagulase activity for human and rabbit fibrinogen, but does not show the activity for rat or guinea pig fibrinogens. This purified protein contains galactose and fucose, and the amino-terminal amino acid sequence was determined. The coagulase activity is inhibited by N-bromosuccinimide (NBS), suggesting that tryptophan is involved in this activity. The coagulase was heat stable to 80 degrees C and stable to pH over the range of 7-9. This is the first report of coagulase from Staphylococcus intermedius.