, Volume 16, Issue 5, pp 497–507 | Cite as

Inhibition of prekallikrein activation in human plasma by components of bovine plasma

  • Kumudini M. Weerasinghe
  • Edward P. Kirby
Original Articles


Contact of plasma with a negatively charged surface activates prekallikrein and factor XII reciprocally. Activation of prekailikrein by several activators was impaired in bovine plasma when compared to that in human plasma. The activated partial thromboplastin time of bovine plasma, induced by several activators, was significantly longer than that of human plasma. Cleavage of [125I]factor XII was optimum at 10 min in human plasma but took up to 60 min in bovine plasma. Addition of bovine plasma to human plasma caused significant inhibition of dextran sulfateinduced prekailikrein activation, indicating that the impaired rate of contact activation in bovine plasma is due to the presence of inhibitors. The inhibitory effect was greater at lower concentrations of dextran sulfate but could not be abolished by increasing the concentration. The inhibitory activity eluted in two peaks at low and medium salt concentrations on carboxymethyl ion-exchange chromatography of bovine plasma.


Public Health Sulfate Internal Medicine Inhibitory Activity Dextran 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.


Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.


  1. 1.
    Margolis, J. 1956. Glass surface and blood coagulation.Nature 178:805–806.Google Scholar
  2. 2.
    Margolis, J. 1969. The interrelationship of coagulation of plasma and release of peptides.Ann. N.Y. Acad. Sci. 00:133–145.Google Scholar
  3. 3.
    Kluft, C. 1977. Assay for prekallikrein levels and prekallikrein activation in human plasma using dextran sulfate as a soluble activator.Thromb. Haemos. 38:220–228.Google Scholar
  4. 4.
    Bock, P. E., K. R. Srinivasan, andJ. D. Shore. 1981. Activation of intrinsic blood coagulation by ellagic acid: Insoluble ellagic acid metal ion complexes are the activating species.Biochemistry 20:7258–7266.Google Scholar
  5. 5.
    Tans, G., andJ. H. Griffin. 1982. Properties of sulfatides in factor XII-dependent contact activation.Blood 59:69–75.Google Scholar
  6. 6.
    Cochrane, C. G., andJ. H. Griffin. 1979. Molecular assembly in the contact phase of the Hageman factor system.Am. J. Med. 67:657–664.Google Scholar
  7. 7.
    Nakayasa, T., andS. Nagasawa. 1979. Studies on human kininogen I. Isolation, characterization, and cleavage by plasma kallikrein of high molecular weight (HMW) kininogen.J. Biochem. 85:249–255.Google Scholar
  8. 8.
    Kaplan, A. 1989. The kallikrein-kinin system in inflammation.Adv. Exp. Med. Biol. 247A:125–135.Google Scholar
  9. 9.
    Saito, H., G. Goldsmith, andO. D. Ratnoff. 1974. Fletcher factor activity in plasmas of various species.Proc. Soc. Exp. Biol. Med. 147:519–523.Google Scholar
  10. 10.
    Claxton, J., W. D. Black, andP. A. Gentry. 1978. Study of TAME (p-tosyl-l-arginine methyl ester) esterase activity in bovine plasma.Am. J. Vet. Res. 39:1235–1238.Google Scholar
  11. 11.
    Weerasinghe, K. M. 1992. Prekallikrein activation in human, bovine and rabbit plasmas; the presence of an inhibitor in bovine plasma.Inflammation 16(3):205–213.Google Scholar
  12. 12.
    Kluft, C. 1988. Synthetic substrates for the assay of prekallikrein and factor XII.Methods Enzymol. 163:170–179.Google Scholar
  13. 13.
    Weerasinghe, K. M., M. F. Scully, andV. V. Kakkar 1983. A platelet derived inhibitor of plasma prekallikrein activation.Thromb. Res. 32:519–529.Google Scholar
  14. 14.
    Kirby, E. P., andP. J. McDevitt. 1983. The binding of bovine F. XII to kaolin.Blood 61:652–659.Google Scholar
  15. 15.
    Bolton, A. E., andW. M. Hunter. 1973. The labelling of proteins to high specific radioactivities by conjugation to a125I-containing acylating agent.Biochem. J. 133:529–539.Google Scholar
  16. 16.
    Laemmli, U. K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4.Nature 227:680–685.Google Scholar
  17. 17.
    Revak, S. D., C. G. Cochrane, A. R. Johnson, andT. E. Hugli. 1974. Structural changes accompanying enzymatic activation of human hageman factor.J. Clin. Invest. 54:619–625.Google Scholar
  18. 18.
    Thornton, R. D., andE. P. Kirby. 1987. Isolation and characterization of an inhibitor of factor XIIa from bovine plasma.J. Biol. Chem. 262:12714–12721.Google Scholar
  19. 19.
    Thornton, R. D., andE. P. Kirby. 1988. Interaction of bovine factor XIIa with an inhibitor from bovine plasma.Biocheim. Biophys. Acta 964:19–27.Google Scholar
  20. 20.
    Revak, S. D., C. G. Cochrane, A. L. Johnston, andT. E. Hugli. 1974. Structural changes accompanying enzymatic activation of human Hageman factor.J. Clin. Invest. 54:619–627.Google Scholar
  21. 21.
    Fujikawa, K., andE. W. Davie. 1981. Human factor XII (Hageman factor).Methods Enzymol. 80:198–211.Google Scholar
  22. 22.
    Fujikawa, K., K. A. Walsh, andE. W. Davie. 1977. Isolation and characterization of bovine F. XII (Hageman factor).Biochemistry 16:2270–2278.Google Scholar
  23. 23.
    Claeys, H., andD. Collen. 1978. Purification and characterization of bovine coagulation factor XII (Hageman factor).Eur. J. Biochem. 87:69–74.Google Scholar
  24. 24.
    Munakata, M., A. Teraoka, Y. Komiyama, M. Masuda, T., Murakami, andK. Murata. 1990. Determination of the minimal concentrations of contact activation factors in deficient substrate plasmas required to assess accurately factor XII, factor XI, factor IX, and high molecular weight kininogen.Thromb. Res. 57:197–203.Google Scholar
  25. 25.
    Saito, H., M. C. Poon, W. Vicie, G. H. Goldsmith, andJ. E. Menitove. 1978. Human plasma prekallikrein (Fletcher factor) clotting activity and antigen in health and disease.J. Lab. Clin. Med. 92:84–95.Google Scholar
  26. 26.
    Bauma, B. N., D. M. Keribiriou, R. A. Vlooswuk, andJ. H. Griffin. 1980. Immunological studies of prekallikrein, kallikrein and high molecular weight kininogen in normal and deficient plasmas and in normal plasma after cold-dependent activation.J. Lab. Clin. Med. 96:693–709.Google Scholar
  27. 27.
    Heimark, R. L., andE. W. Davie. 1979. Isolation and characterization of bovine plasma prekallikrein (Fletcher factor).Biochemistry 18:5743–5750.Google Scholar
  28. 28.
    Nossel, H. L., H. Rubin, M. Drillings, andR. Hsieh. 1968. Inhibition of Hageman factor activation.J. Clin. Invest. 47:1172–1180.Google Scholar
  29. 29.
    Weerasinghe, K. M., M. F. Scully, andV. V. Kakkar. 1984. Inhibition of the cerebroside sulphate (sulfatide) induced contact activation reactions by platelet factor-4.Thromb. Res. 33:625–631.Google Scholar
  30. 30.
    Kodama, K., H. Kato, andS. Iwanaga. 1985. Isolation of bovine platelet cationic proteins which inhibit the surface-mediated activation of Factor XII and prekailikrein.J. Biochem. 97:139–151.Google Scholar
  31. 31.
    Oh-Ishi, S., M. Katori, Y. N. Han, S. Iwanaga, H. Kato, andT. Suzuki. 1977. Possible physiological role of new peptide fragments released from bovine high molecular weight kininogen by plasma kailikrein.Biochem. Pharmacol. 26:115–120.Google Scholar

Copyright information

© Plenum Publishing Corporation 1992

Authors and Affiliations

  • Kumudini M. Weerasinghe
    • 1
  • Edward P. Kirby
    • 2
  1. 1.Department of Anatomy, Physiological Sciences and Radiology, College of Veterinary MedicineNorth Carolina State UniversityRaleigh
  2. 2.Department of BiochemistryTemple University School of MedicinePhiladelphia

Personalised recommendations