Apropos Aprotinin: A Review

Access optionsAccess options

Rent or Buy article

Get time limited or full article access on ReadCube.


All prices are NET prices.


  1. 1

    Hansen, J., Billich, S., Schulze, T., Sukrow, S. and Moelling, K. 1988. Partial purification and substrate analysis of bacterially expressed HIV proteases by means of monoclonal antibody. EMBO J. 7: 1785–1791.

  2. 2

    Allen, P.M. 1987. Antigen processing at the molecular level. Immunol. Today 8: 270–273.

  3. 3

    Kunitz, M. and Northrop, J.H. 1936. Isolation from beef pancreas of crystalline trypsinogen, trypsin, trypsin inhibitor, and an inhibitor trypsin compound. J. Gen. Physiol. 19: 991–1007.

  4. 4

    Fritz, H. and Wunderer, G. 1983. Biochemistry and applications of aprotinin, the Kallikrein inhibitor from bovine organs. Arzneim. Forsch./Drug Res. 33: 479–494.

  5. 5

    Hochstrasser, K. and Wachter, E. 1980. A new Kunitz-type inhibitor from bovine serum: amino acid sequence determination. FEBS Lett. 119: 58–62.

  6. 6

    Frey, E.K., Kraut, H. and Werle, E. (Eds.). 1968. Das Kallikrein-kinin-system und seine inhibitoren, pp. 114–142. F. Enke-Verlag, Stuttgart, F.R.G.

  7. 7

    Zyznar, E.S. 1981. A rationale for the application of trasylol as a protease inhibitor in radioimmunoassay. Life Sci. 28: 1861–1866.

  8. 8

    Hafeli, R. 1981. U.S. Patent 4,259,447.

  9. 9

    Johnson, D.A. and Travis, J. 1976. Rapid purification of human trypsin and chymotrypsin I. Anal. Biochem. 72: 573–576.

  10. 10

    Beck, E.A., Bachmann, P., Barbier, P. and Furlan, M. 1976. Importance of protease inhibition in studies on purified factor VIII (antihemophilic factor) Thromb. Haemostasis. 35: 186–190.

  11. 11

    Andersson, A., Eriksson, U. and Ostenson, C.G. 1981. Glucagon production by cultured pancreatic islets: effects of different culture conditions and media. In Vitro 17: 378–384.

  12. 12

    Amundsen, E., Putter, J., Friberger, P., Knos, M., Lardsbraten, M. and Claesen, G. 1979. Methods for the determination of glandular Kallikrein by means of a chromo-genic tripeptide substrate. Adv. Expt. Med. Biol. 120A: 83–95.

  13. 13

    Matas, A.J., Sutherland, D.E.R., Steffens, M.W. and Narajian, J.S. 1976. Short-term culture of adult pancreatic fragments for purification and transplantation of islets of Langerhans. Surgery 80: 183–191.

  14. 14

    Wunschmann–Henderson, B., Horwitz, D.L. and Astrup, T. 1972. Release of plas-minogen activator from viable leukocytes of man, baboon, dog, and rabbit. Proc. Soc. Exp. Biol. Med. 141: 634–638.

  15. 15

    Murakami, H. 1989. Serum-free media used for cultivation of hybridomas. In: Monoclonal Antibodies: Production and Application, pp. 107–141. Alan Liss, Inc., NY.

  16. 16

    Cook, J.R. and Chen, J.-K. 1988. Enhancement of transformed cell growth in agar by serine protease inhibitors. J. Cell. Physiol. 136: 188–193.

  17. 17

    Karl, D.W., Bohn, M.A. and Flickinger, M.C. Cleavage of murine IgG2a by an acid proteinase released by hybridoma cells: acid protease from mouse hybridoma. Abstract, Am. Chem. Soc., 196th Meeting.

  18. 18

    Offord, R.E., Philippe, J., Davis, J.G., Halban, P.A. and Berger, M. 1979. Inhibition of degradation of insulin by ophthalmic acid and by a bovine pancreatic proteinase inhibitor. Biochem. J. 182: 249–251.

  19. 19

    Goldberg, A.R. and Lazarowitz, S.G. 1974. Plasminogen activators of normal and transformed cells. In: Bayer Symposium V, Proteinase Inhibitors. Fritz, H., Tschesche, H., Greene, L. J., and Truscheit, E. (Eds.), pp. 631–648. Springer-Verlag, New York.

  20. 20

    Nakamura, T., Asami, O., Tanaka, K. and Ichihara, A. 1984. Increased survival of rat hepatocytes in serum-free medium by inhibition of a trypsin-like protease associated with their plasma membranes. Exp. Cell. Res. 154: 81–91.

  21. 21

    Asami, O.T., Nakamura, T., Mura, T. and Ichihara, A. 1984. Identification of trypsin inhibitor in bovine pituitary extracts as a survival factor for adult rat hepatocytes in primary culture. J. Biochem. 95: 299–309.

  22. 22

    Davis, H., Gasco, C. and Kiernan, J.A. 1976. Effects of aprotinin on organ cultures of the rat's kidney. In Vitro. 12: 192–197.

  23. 23

    Hirschhorn, R., Grossman, J., Troll, W. and Weissman, G. 1971. The effects of epsilon amino caproic acid and other inhibitors of proteolysis upon the response of human peripheral blood lymphocytes to phytohemagglutinin. J. Clin. Invest. 50: 1206–1217.

  24. 24

    Hart, D.A. 1977. The effect of soybean trypsin inhibitor on concanavalin A and phytohemagglutinin stimulation of hamster, guinea pig, rat, and mouse lymphoid cells. Cell. Immunol. 32: 146–159.

  25. 25

    Vischer, T.L. 1979. Protease inhibitors reduce mitogen-induced lymphocyte stimulation. Immunol. 36: 811–813.

  26. 26

    Higuchi, S., Ohkawara, S., Nakamura, S. and Yoshinaga, M. 1977. The polyvalent protease inhibitor, trasylol, inhibits DNA synthesis of mouse lymphocytes by an indirect mechanism. Cell. Immunol. 34: 395–405.

  27. 27

    Hunt, L.T., Barber, W.C. and Daghoff, M.O. 1974. Epidermal growth factor: internal duplication and probable relationship to pancreatic secretory trypsin inhibitor. Biochim. Biophys. Res. Commun. 60: 102–1028.

  28. 28

    Eaton, D.L. and Baker, J.B. 1983. Evidence that a variety of cultured cells secrete protease nexin and produce a distinct cytoplasmic serine-protease binding factor. J. Cell. Physiol. 117: 175–182.

  29. 29

    Knauer, D.J. and Cunningham, D.D. 1984. Protease nexins: cell-secreted proteins which regulate extracellular serine proteases. Trends. Biochem. Sci. 9: 231–233.

  30. 30

    Edwards, D.R., Murphy, G., Reynolds, J.J., Whitman, S.E., Dochertz, A.J.P., Angel, P. and Heath, J.K. 1987. Transforming growth factor beta modulates the expression of collagenase and metalloprotemase inhibitor. EMBO J. 6: 1899–1904.

  31. 31

    Hawkins, R.L. and Seeds, N.W. 1986. Effect of proteases and their inhibitors on neurite outgrowth from neonatal mouse sensory ganglia in culture. Brain Res. 398: 63–70.

  32. 32

    Fischer, G. 1982. Cultivation of mouse cerebellar cells in serum-free, hormonally defined media: survival of neurons. Neurosci. Lett. 28: 325–329.

  33. 33

    Catalioto, R.M., Negrel, R., Gaillard, D. and Ailhaud, G. 1987. Growth-promoting activity in serum-free medium of Kallikrein-like arginylesteropeptidases from rat sub-maxillary gland. J. Cell. Physiol. 130: 352–360.

  34. 34

    Kramer, M.D., Fruth, U., Simon, H.-G. and Simon, M.M. 1989. Expression of cytoplasmic granules with T cell-associated serine proteinase activity in Ly-2+ (CD8+) T lymphocytes responding to lymphocytic choriomeningitis virus in vivo. Eur. J. Immunol. 19: 151–156.

  35. 35

    Auberger, P., Mary, D., Breittmayer, J.-P., Aussel, C. and Fehlmann, M. 1989. Chymotryptic-type protease inhibitors block the increase in Ca2+ and IL-2 production in activated Jurkat T cells. J. Immunol. 142: 1253–1259.

  36. 36

    Barnes, D.W., McKeehan, W.L. and Sato, G.H. 1987. Cellular endocrinology: integrated physiology in vitro. In Vitro Cell. Dev. Biol. 23: 659–662.

  37. 37

    Barnes, D., Sirbasku, D.A. and Sato, G.H. (Eds.). 1984. Cell Culture Methods for Molecular and Cell Biology, Vol. 1–4. Alan R. Liss, New York.

  38. 38

    Bodecker, B.G.D., Berg, G.J., Hewlett, G. and Schlumberger, H.D. 1985. A screening method to develop serum-free culture media for adherent cell lines. Dev. Biol. Stand. 60: 93–99.

  39. 39

    Maurer, H.R. 1986. Towards chemically-defined, serum-free media for mammalian cell culture. In: Animal Cell Culture: A Practical Approach. Freshney, R.I. (Ed.) pp. 13–31. IRL Press, Oxford, U.K.

  40. 40

    Freshney, R.I. 1987. Culture of Animal Cells: A Manual of Basic Technique. Alan R. Liss, New York.

  41. 41

    Hewlett, G. 1988. Zellkulturen und der einsatz von serumfreien medien. BioEng. 4/88: 110–112.

Download references

Author information

Rights and permissions

Reprints and Permissions

About this article

Further reading