Modification of Trypsin Pancreatic Inhibitor by Polysaccharides for Prolongation of Therapeutic Effect

  • N. I. Larionova
  • I. Y. Sakharov
  • N. F. Kazanskaya
  • A. G. Zhuravlyov
  • V. G. Vladimirov
  • P. I. Tolstich


A polyvalent inhibitor of proteinases from the bovine pancreas effectively blocks the action of kallikrein, chymotrypsin, plasmin, plasmin activator, blood coagulation factors, and tissue and leukocytic proteinases (1). Owing to its wide specificity, this pancreatic inhibitor has long been used in therapeutic practice (2, 3). The great variety of the modes of action of the pancreatic inhibitor on the organism is illustrated by the list of possible targets for its curative effect (Fig. 1). This inhibitor is used in treating diseases associated with activation of the kinin systems in the organism (5). Such diseases include acute pancreatitis, primary hyperfibrinolytic hemorrhage and coagulopathy, burns, nephrotic syndrome, and shock of different etiology (4,6). Pancreatic inhibitor is very effective in normalizing the indices of the kinin system when large doses of this expensive preparation are used with these diseases. Large doses are needed because the inhibitor does not persist in the blood flow. The half-life of pancreatic inhibitor is 7 to 10 min depending on the species of the animal and on the dose (4,7). Also, it is desirable to maintain a high concentration of pancreatic inhibitor in the blood to prolong the inhibition.


Acute Pancreatitis Native Inhibitor Cyanuric Chloride Blood Coagulation Factor DEAE 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.
    Vogel, R., Trautschold, I. & Werle, E. “Natural Proteinase Inhibitors”, Academic Press, New York, 1968.Google Scholar
  2. 2.
    Marx, R., Imdahl, H. & Haberland, G. L. “Neue Aspekte der Trasylol Therapie”, Schattauer-Verlag, Stuttgart, 1968.Google Scholar
  3. 3.
    Werle, E., In “Proceedings of the International Research Conference on Proteinase Inhibitors” (Ed. H. Fritz and H. Tschesche, eds.) Walter de Gruyter, Berlin, 1971, p. 23.Google Scholar
  4. 4.
    Veremeenko, K. N. “Enzymes of Proteolysis and Their Inhibitors in Medical Practice” (Russ.), Kiev, 1971.Google Scholar
  5. 5.
    Paskhina, T. S. & Menshikov, V. V. “Kinins and Kinin Blood System: Sbornik Nauchnik Trudov” (Russ.), First I. M. Sechenov Med. Inst., Moscow, 1976.Google Scholar
  6. 6.
    Paskhina, T. S., Dolgina, N. I., Nartikova, V. F., Krinskaja, A. B., Morosova, N. A. & Rossinskaya, E. V. Med. Chimii (Russ.) 23: 689, 1977.Google Scholar
  7. 7.
    Fritz, H., Oppitz, K.-H., Meckl, D., Kemkes, B., Haendle, H., Schult, H. & Werle, E. Hoppa-Seyler. Z. Physiol. Chem. 350: 1541, 1969.CrossRefGoogle Scholar
  8. 8.
    Broun, G., In “Enzyme Engineering” vol 2 (E. K. Pye and L. B. Wingard, Jr., eds) Plenum Press, New York, 1974, p. 433.Google Scholar
  9. 9.
    Marshall, J. J. Trends Biochem. Sci. 3: 79, 1978.CrossRefGoogle Scholar
  10. 10.
    Berezin, I. V., Antonov, V. K. & Martinek, K. “Immobilizovannye Fermenty” (“Immobilized Enzymes”), Moscow University Press, Moscow, 1975.Google Scholar
  11. 11.
    Larionova, N. I., Kazanskaya, N. F. & Sakharov, I. Y. Biochemistry (Russ.) 42: 1237, 1977.Google Scholar
  12. 12.
    Larionova, N. I., Kazanskaya, N. F. & Sakharov, I. Y. Biochemistry (Russ.) 43: 880, 1978.Google Scholar
  13. 13.
    Chauvet, J. & Acher, R. J. Biol. Cham. 242: 4274, 1976.Google Scholar
  14. 14.
    Larionova, N. I., Kazanskaya, N. F. & Sakharov, I. Y. Biochemistry (Russ.) 44: 350, 1979.Google Scholar
  15. 15.
    Luthy, J. A., Praissman, M., Finkenstadt, W. R. & Laskowski, M. Jr. J. Biol. Chem. 248: 1760, 1973.Google Scholar
  16. 16.
    Abukhovsky, A., Van Es, T., Palczuk, N. C. & Davis, F. F. J. Biol. Chem. 252: 3578, 1977.Google Scholar
  17. 17.
    Sherwood, R. F., Baird, J. K., Atkinson, T., Wiblin, C. N., Rutter, D. A. & Ellwood, D. C. Biochem. J. 164: 461, 1977.Google Scholar
  18. 18.
    Pratten, M. K., Duncan, R. & Lloyd, J. B. Biochem. Blopkys. Acta 540: 455, 1978.CrossRefGoogle Scholar

Copyright information

© Plenum Press, New York 1980

Authors and Affiliations

  • N. I. Larionova
    • 1
  • I. Y. Sakharov
    • 1
  • N. F. Kazanskaya
    • 1
  • A. G. Zhuravlyov
    • 1
  • V. G. Vladimirov
    • 1
  • P. I. Tolstich
    • 1
  1. 1.N. I. Pirogov Second State Medical InstituteMoscow State UniversityMoscowUSSR

Personalised recommendations