Characterization of the interaction of bovine plasmin with Streptococcus uberis

J Appl Microbiol. 1998 Jun;84(6):1104-10. doi: 10.1046/j.1365-2672.1998.00452.x.


The binding of plasmin to Streptococcus uberis strain 0140 J was optimal in the pH range 5.0-5.5. Plasmin binding decreased exponentially with increasing NaCl concentration (0-0.8 mol l-1), reaching a minimum at NaCl concentrations exceeding 0.55 mol l-1. Neither K+, Mg2+ nor the metal chelator EDTA had any effect on the interaction. Plasmin binding was prevented, in a concentration-dependent manner, by the amino acids lysine, arginine and epsilon-aminocaproic acid. Bound plasmin was also eluted from the bacterial cell using the same amino acids. Bound plasmin was lost from the bacterium in a time- and temperature-dependent fashion, the rate of plasmin loss increased with increasing temperature over the range 4-55 degrees C, and the elution of plasmin from live and heat-killed bacteria was similar. Cell-bound plasmin was only partially inhibited by the physiological inhibitor alpha 2-antiplasmin whereas the serine protease inhibitor aprotinin, and the active site titrant p-nitrophenyl-p-guanidiniobenzoate, inhibited the activity of the cell-bound plasmin by more than 95%.

MeSH terms

  • Aminocaproates / pharmacology
  • Animals
  • Arginine / pharmacology
  • Cattle
  • Dose-Response Relationship, Drug
  • Edetic Acid / pharmacology
  • Fibrinolysin / analysis
  • Fibrinolysin / metabolism*
  • Hot Temperature
  • Hydrogen-Ion Concentration
  • Lysine / pharmacology
  • Magnesium / pharmacology
  • Osmolar Concentration
  • Potassium / pharmacology
  • Protease Inhibitors / pharmacology
  • Streptococcus / metabolism*
  • Temperature
  • Time Factors


  • Aminocaproates
  • Protease Inhibitors
  • Arginine
  • Edetic Acid
  • Fibrinolysin
  • Magnesium
  • Lysine
  • Potassium