Some Properties of an Antiplasmin Substance from Rabbit Platelets

Summary

Rabbit platelets contained a proteinase inhibitor which inhibited plasmin, trypsin and chymotrypsin activities, and serum kallikrein to some extent. It did not inhibit pancreatic kallikrein and thrombin. It reacted stoechiometrically with these enzymes in a prompt fashion and was found to have a molecular weight of about 40,000.

• References

• 1 Johnson S. A, Schneider G. L. The existence of antifibrinolysin activity in platelets. Science 117: 229 1953;
• 2 Stefanini M, Murphy I. S. Studies on platelets. XIV. Human platelets as source of antifibrinolysin. J. clin. Invest 35: 355 1956;
• 3 Sherry S, Alkjaersig N. Studies on the fibrinolytic enzyme of human plasma. Thrombos. Diathes. haemorrh. (Stuttg.) 01: 264 1957;
• 4 Holemans R, Gross R. Influence of blood platelets on fibrinolysis. Thrombos. Diathes. haemorrh. (Stuttg.) 06: 196 1961;
• 5 Osuga T, Wakabayshi K, Matsuda M, Kazama M, Abe T. Inhibitory effect of blood platelet on plasma fibrinolytic activity. Jap. J. clin. Hematol 09: 504 1968;
• 6 Nagasawa S, Suzuki T. A simple method for purification of bovine plasminogen. J. Biochem. (Tokyo) 66: 273 1969;
• 7 Yano M, Nagasawa S, Suzuki T. Purification and properties of bovine serum kallikrein activated with casein. J. Biochem. (Tokyo). in press.
• 8 Blombäck B, Blombäck M. Purification of human and bovine fibrinogen. Arkiv Kemi 10: 415 1956;
• 9 Berg W, Korsan-Bengsten K. Separation of human fibrinogen and plasminogen by means of gel filtration. Thrombos. Diathes. haemorrh. (Stuttg.) 09: 151 1963;
• 10 Remmert L. F, Cohen P. P. Partial purification and properties of a proteolytic enzyme of human serum. J. biol. Chem 181: 431 1949;
• 11 Ghan N. M, Mertz E. T. Studies on plasminogen. V. Purification of bovine and human plasminogens by Sephadex chromatography. Canad. J. Biochem 44: 475 1966;
• 12 Roberts P. S. Measurement of the rate of plasmin action on synthetic substrates. J. biol. Chem 232: 285 1958;
• 13 Lowry O. H, Rosenbangh N. J, Fan A. L, Randall R. J. Protein measurement with the Folin phenol reagent. J. biol. Chem 193: 265 1951;
• 14 Whitacker J. R. Determination of molecular weights of proteins by gel filtration on Sephadex. Anal. Chem 35: 1950 1963;
• 15 Wu F. G, Laskowski M. Crystalline acid-labile trypsin inhibitor from bovine blood plasma. J. biol. Chem 235: 1680 1960;
• 16 Martin G. J. Inhibition of trypsin, chymotrypsin, and plasmin by an inhibitor isolation from sheep serum. J. biol. Chem 237: 2099 1962;
• 17 Schönenberger M, Schmidtberger R, Schultz H. E. Über das α₂-Makroglobulin. Z. Naturforsch 136: 761 1958;
• 18 Haverback B. J, Dyce B, Bundy H. F, Wirtschafter S. K, Edmondson H. A. Protein binding of pancreatic proteolytic enzymes. J. clin. Invest 41: 972 1962;
• 19 Ganrot P. O. Interaction of plasmin and trypsin with α₂-macroglobulin. Acta chim. scand 21: 602 1967;
• 20 Nagasawa S, Han B. H, Sugihara H, Suzuki T. Studies on α₂-macroglobulin in bovine plasma. I. Purification, physical properties, and chemical composition. J. Biochem. (Tokyo). (In press)
• 21 Nagasawa S, Han B. H, Sugihara H, Suzuki T. Studies on α₂-macroglobulin in bovine plasma. II. Interaction of α₂-macroglobulin and trypsin. J. Biochem. (Tokyo). (In press)
• 22 Vogel R, Trautshold I, Werle E. Natürliche Proteinasen-Inhibitoren. Weitzel G, Zöllner N. Thieme; Stuttgart: 1966
• 23 Jürgens J, Pryzbilski R. Antifibrinolytic activity of platelets. Exp. Biol. Med 03: 181 1968;
• 24 McDonagh J, Kiesselbach T. H, Wagner R. H. Factor XIII and antiplasmin activity in human platelets. Amer. J. Physiol 216: 508 1969;
• 25 Lorand L, Konishi K. Activation of the fibrin stabilizing factor of plasma by thrombin. Arch. Biochem 105: 58 1964;
• 26 Warburg O, Christian W. Isolierung und Kristallisation des Gärungsferments Enolase. Biochem. Z 310: 384 1942;