Kinins IV pp 161-166 | Cite as

Kininogen by the SRI Method in Human Serum During an Acute Phase Inflammatory Reaction

  • Ulla Hamberg
  • Tytti Kärkkäinen
  • Thomas Tallberg
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 198A)


The concentration of several serum proteins changes during the acute phase in inflammatory states.1 Kininogen belongs to this group of acute phase reactants as shown in our earlier studies and also with plasma from patients with rheumatoid arthritis.2 In early studies plasma kininogen was measured exclusively by estimation of the bradykinin equivalent by bio- assay on the isolated rat uterus or guinea pig ileum. 3 More recently a bradykinin enzyme immunoassay4, radioimmunoassay5 and rocket Immunoelectrophoresis6 were reported for the determination of HMr kininogen in plasma. A method designated to determination of the total plasma and serum kininogen by single radial immunodiffusion (SRI) was recently presented by us in detail.7 The SRI method was compared with and correlated to kininogen determined by the bradykinin equivalent and gives the corresponding normal values in human plasma and serum. This presentation deals with its application in a study of kininogen investigated in a serum material collected from patients during periods of treatment with immunotherapy in renal cell carcinoma.8–12 An infiammatory reaction provoked during the treatment was shown by the increase of a1-acid glycoprotein and some other acute phase reactants.


Renal Cell Carcinoma Patient Seron Plasma Kallikrein High Molecular Weight Kininogen Active Specific Immunotherapy 
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.
    A. Koj, Acute-phase reactants, in: “Structure and Function of Plasma Proteins,” A. C. Allison, ed., Plenum Publishing Corporation (1974).Google Scholar
  2. 2.
    J. N. Sharma, J. J. Zeitlin, P. M. Brooks, W. W. Buchman, and W. C. Dick, The action of aspirin on plasma kininogen and other plasma proteins in rheumatoid patients: Relationship to disease activity, Clin. Exp. Pharmacol. Physiol., 1: 347–354 (1980).CrossRefGoogle Scholar
  3. 3.
    C. G. Cochrane and J. H. Griffin, The biochemistry and pathophysiology of the contact system in plasma, Adv. Immuno., 33: 241–306 (1982).CrossRefGoogle Scholar
  4. 4.
    A. Ueno, S. Oh-Ishi, T. Kitagawa, and M. Katori, Enzyme immunoassay of bradykinin, Adv. Pxp. Med. Biol., 120A: 195–202 (1979).Google Scholar
  5. 5.
    D. Proud, J. V. Pierce, and J. J. Pisano, Radioimmunoassay of human high molecular weight kininogen in normal and deficient plasma, J. Lab. Clin. Med., 95: 563–574 (1980).PubMedGoogle Scholar
  6. 6.
    B. N. Bouma, D. M. Kerbiriou, R. A. A. Vlooswijk, and J. H. Griffin, 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 (1980).PubMedGoogle Scholar
  7. 7.
    U. Hamberg and T. Karkkainen, Determination of human plasma kininogen by a single radial immunodiffusion method and the bradykinin equivalent, Clin. Chim. Acta, 142: 211–220 (1984).CrossRefGoogle Scholar
  8. 8.
    Th. Tallberg, Cancer immunotherapy by means of polymerized autologous tumour tissue with special reference to some patients with pulmonary tumour, Scand. J. Respir. Pis. Suppl., 89 (1974).Google Scholar
  9. 9.
    H. Tykkä, Active specific immunotherapy with supportive measures in the treatment of advanced palliatively nephrectomized renal adenocarcinoma. A controlled clinical study, Academic dissertation, Scand. J. Urol. & Neephrol. Suppl., 63 (1981).Google Scholar
  10. 10.
    H. Tykka, K. Oravisto, M. Turunen, and Th. Tallberg, Disappearance of lung metastases during immunotherapy in five patients juffering from renal carcinoma, Scand. J. Respir. Dis., 123, Suppl. 89 (1974).Google Scholar
  11. 11.
    H. Tykkä, K. Oravisto, T. Lehtonen, S. Sarna, and Th. Tallberg, Active specific immunotherapy of advanced renal-cell carcinoma, Eur. Urol., 4: 250 (1978).PubMedGoogle Scholar
  12. 12.
    J. A. Neidhart, S. G. Murphy, L. A. Hennick, and H. A. Wise Active specific immunotherapy of stage IV renal cell carcinoma with aggregated tumour antigen adjuvant, Cancer, 46: 1128 – 1134 (1980).PubMedCrossRefGoogle Scholar
  13. 13.
    A.-C. Syvanen, T. Karkkainen, and U. Hamberg, Conformation and sequence dependent determinants of human low molecular weight kininogen, Molec. Immunol., 20: 669–678 (1983).Google Scholar
  14. 14.
    U. Hamberg, Kininogen in human plasma after fibrinolytic activation, Scand. J. Clin. Lab. Invest. Suppl., 107: 37–47 (1969).PubMedGoogle Scholar
  15. 15.
    S. Suzuki, T. Murakoshi, and W. Sakamoto, Studies on the various causal factors related to hypercoagulability in the field of obstetrics with special reference to the onset of DIC as viewed from the changing of kinin-kallikrein system and fibrinopeptide A, Adv. Exp. Med. Biol., 156A: 1055–1065 (1983).PubMedGoogle Scholar
  16. 16.
    M. Maki, K. Soga, and K. Gotoh, The kinin-forming enzyme system in pregnancy and obstetrical DIC, in: “Disseminated Intravascular Coagulation,” T. Abe and M. Yamaka, eds., Karger, Bibliotheca Haematologica, 49:239–246 (1983).Google Scholar

Copyright information

© Plenum Press, New York 1986

Authors and Affiliations

  • Ulla Hamberg
    • 1
  • Tytti Kärkkäinen
    • 1
  • Thomas Tallberg
    • 2
  1. 1.Department of BiochemistryUniversity of HelsinkiHelsinki 17Finland
  2. 2.Laboratory of ImmunologyHelsinki University Central HospitalHelsinki 28Finland

Personalised recommendations