Advertisement

Kinins pp 135-150 | Cite as

Bovine Plasma HMW and LMW Kininogens: Isolation and Characterization of the Polypeptide Fragments Produced by Plasma and Tissue Kallikreins

  • H. Kato
  • Y. N. Han
  • S. Iwanaga
  • T. Suzuki
  • M. Komiya
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 70)

Abstract

There exist at least two types of kininogens with different molecular weight in mammalian blood plasmas, which are named high molecular weight (HMW) and low molecular weight (LMW) kininogens (1). Although their functions in kallikrein-kinin system remain to be investigated, it has been speculated that HMW kininogen participates in the intrinsic kinin releasing system and Imw kininogen in the extrinsic kinin-releasing system. Quite recently, a new function of kininogen has been suggested by findings of Flaujeac (2), Williams (3), and Fitzgerald (4) traits with a deficiency of kininogen. These plasmas do not release kinin appreciably upon incubation of plasma kallikrein and also has a prolonged activated partial thromboplastin time and inability to form plasmin. These facts suggest the participation of the kininogen in the intrinsic blood coagulation and fibrinolysis, in addition to the kinin-forming system.

Keywords

High Molecular Weight Snake Venom Void Volume Fraction Tissue Kallikrein Plasma Kallikrein 
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.

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  1. 1.
    Habermann, E. (1970) in: Handbook of Experimental Pharmacology (Erdos, E.G., ed.) pp. 250–288, Springer-Verlag, Berlin-Heidelberg-New York.Google Scholar
  2. 2.
    Wuepper, K.D., Miller, D.R. and Lacomb, M.J. (1975) Federation Proc. 34, 859.Google Scholar
  3. 3.
    Colman, R.W., Badasarian, A., Talamo, R.C., Seavey, M., Scott, C.F. and Kaplan, A.P. (1975) Federation Proc. 34, 859.Google Scholar
  4. 4.
    Saito, H., Ratnoff, O.D., Waldmann, R. and Abraham, J.P. (1975) J. Clin. Invest. 55, 1082–1089.PubMedCrossRefGoogle Scholar
  5. 5.
    Komiya, M., Kato, H. and Suzuki, T. (1974) J. Biochem. 76, 811–822.PubMedGoogle Scholar
  6. 6.
    Komiya, M., Kato, H., and Suzuki, T. (1974) J. Biochem. 76, 833–845.PubMedGoogle Scholar
  7. 7.
    Komiya, M., Suzuki, T. and Han, Y.N. (1973) Seikagaku (in Japanese) 45, 682.Google Scholar
  8. 8.
    Han, Y.N., Komiya, N., Iwanaga, S. and Suzuki, T. (1975) J. Biochem. 77, 55–68.PubMedGoogle Scholar
  9. 9.
    Yano, M., Kato, H., Nagasawa, S. and Suzuki, T. (1967) J. Biochem. 62, 386–388.PubMedGoogle Scholar
  10. 10.
    Takahashi, H., Nagasawa S. and Suzuki, T. (1972) J. Biochem. 71, 471–483.PubMedGoogle Scholar
  11. 11.
    Komiya, M., Nagasawa, S. and Suzuki, T. (1972) J. Biochem. 72, 1205–1218.PubMedGoogle Scholar
  12. 12.
    Iwanaga, S., Sata, T., Mizushima, Y. and Suzuki, T. (1965) J. Biochem. 58, 123–129.PubMedGoogle Scholar
  13. 13.
    Yano, M., Nagasawa, S. and Suzuki, T. (1971) J. Biochem. 69, 471–481.PubMedGoogle Scholar
  14. 14.
    Spackman, D.H., Stein, W.H. and Moore, S. (1958) Anal. Biochem. 30, 1190–1206.Google Scholar
  15. 15.
    Edman, P. (1970) in: Protein Sequence Determination (Needleman, S.B., ed.) pp. 211-255, Springer-Verlag, Berlin.Google Scholar
  16. 16.
    Bailey, J.L. (1967) in: Techniques in Protein Chemistry, 2nd ed., pp. 163–182, Elsevier, New York.Google Scholar
  17. 17.
    Braun, V. and Schroeder, W.A. (1967) Arch. Biochem. Biophys. 118, 241–252.CrossRefGoogle Scholar
  18. 18.
    Dubois, M., Gilles, K.A., Hamilton, J.K., Rebers, P.A. and Smity, F. (1956) Anal. Chem. 28, 350–356.CrossRefGoogle Scholar
  19. 19.
    Gardell, S. (1953) Acta Chem. Scand. 7, 207–215.CrossRefGoogle Scholar
  20. 20.
    Warren, L. (1959) J. Biol. Chem. 234, 1971–1975.PubMedGoogle Scholar
  21. 21.
    Weber, K. and Osborn, M. (1969) J. Biol. Chem. 244, 4406–4412.PubMedGoogle Scholar
  22. 22.
    Kato, H., Nagasawa, S. and Suzuki, T. (1967) Biochem. Biophys. Res. Communs. 27, 163–168.CrossRefGoogle Scholar
  23. 23.
    Iwanaga, S., Han, Y.N., Komiya, M., Suzuki, T. Katori, N., Ohishi, S. (1975) Life Science 16, 792–793.CrossRefGoogle Scholar
  24. 24.
    Nagasawa, S., Mizushima, Y., Sata, T., Iwanaga, S. and Suzuki, T. (1966) J. Biochem. 60, 643–652.PubMedGoogle Scholar
  25. 25.
    Goodwin, T.W. and Morton, R.A. (1946) Biochem. J. 40, 628–632.Google Scholar

Copyright information

© Plenum Press, New York 1976

Authors and Affiliations

  • H. Kato
    • 1
  • Y. N. Han
    • 1
  • S. Iwanaga
    • 1
  • T. Suzuki
    • 1
  • M. Komiya
    • 1
  1. 1.Institute for Protein ResearchOsaka UniversitySuita, OsakaJapan

Personalised recommendations