Skip to main content
SpringerLink
Log in

Trypsin- und Chymotrypsin-Inhibitoren in Leguminosen

VII. Partialsequeuzen des Trypsin-Chymotrypsin-Inhibitors PCI 3 aus Phaseolus coccineus

Trypsin and chymotrypsin inhibitors in leguminosae

VII. Partial amino acid sequences of the trypsin chymotrypsin inhibitor PCI 3 from Phaseolus coccineus

  • Published:
Zeitschrift für Lebensmittel-Untersuchung und Forschung Aims and scope Submit manuscript

Summary

The sequences of amino acid residues at the amino and carboxyl terminus and around the reactive sites of the trypsin chymotrypsin inhibitor PCI 3 from the seeds of runner beans (Phaseolus coccineus L.) were estimated by aminopeptidase O and carboxypeptidase A degradation before and after enzymatical modification with trypsin or chymotrypsin. Beginning at the amino terminus the sequences are: Ser-Glu-Ala-Gly-Gln-..., ...-Ile-Tyr-Lys-Ser-Gln-(Pro)-... with Lys-Ser as reactive site against trypsin, ...-Asp-Val-Ala-Leu-Ser-(Pro)-... with Leu-Ser as reactive site againstα-chymotrypsin, and ...-Thr-Arg-Ala-Lys-Phe-Leu as C-terminus. The importance of the serine residue in the reactive sites concerning the specificity of inhibitors is dicussed.

Zusammenfassung

Die Aminosäuresequenzen am N- und C-Terminus und um die reaktiven Zentren des Trypsin-Chymotrypsin-Inhibitors PCI 3 aus den Samen von Feuerbohnen (Phaseolus coccineus L.) wurden durch Abbau mit Aminopeptidase O und Carboxypeptidase A vor und nach der enzymatischen Modifizierung mit Trypsin oder Chymotrypsin bestimmt. Beginnend am N-Terminus wurden folgende Sequenzen gefunden: Ser-Glu-Ala-Gly-Gln..., ...-Ile-Tyr-Lys-Ser-Gln-(Pro)-... mit Lys-Ser als reaktivem Zentrum gegen Trypsin, ...-Asp-Val-Ala-Leu-Ser-(Pro)-... mit Leu-Ser als reaktivem Zentrum gegenα-Chymotrypsin und ...-Thr-Arg-Ala-Lys-Phe-Leu als C-Terminus. Die Bedeutung des Serinrestes in den reaktiven Zentren für die Spezifität der Inhibitoren wird diskutiert.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Log in via an institution

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Institutional subscriptions

Similar content being viewed by others

Literatur

  1. Weder,J.K.P., Kassubek,A., Hory,H.-D.: Chem. Mikrobiol. Technol. Lebensm.4, 79 (1975)

    Google Scholar 

  2. Weder,J.K.P., Hory,H.-D.: Chem. Mikrobiol. Technol. Lebensm.4, 161 (1976)

    Google Scholar 

  3. Hory,H.-D., Weder,J.K.P., Belitz,H.-D.: Z. Lebensm. Unters.-Forsch. (im Druck)

  4. Hochstrasser,K., Illchmann,K., Werle,E., Hössl,R., Schwarz,S.: Hoppe-Seyler's Z. physiol. Chem.351,1503 (1970)

    Google Scholar 

  5. Tan,C.G.L., Stevens,F.C.: Eur. J. Biochem.18, 515 (1971)

    PubMed  Google Scholar 

  6. Odani, S., Ikenaka, T.: J. Biochem. (Tokyo)71, 839 (1972)

    Google Scholar 

  7. Koide,T., Tsunasawa,S., Ikenaka,T.: J. Biochem. (Tokyo)71, 165 (1972)

    Google Scholar 

  8. Stevens,F.C., Wuerz,S., Krahn,J.: Structure-function relationships in lima bean protease inhibitor. In: Bayer-Symposium V: Proteinase Inhibitors, Grosse Ledder near Cologne, FRG, Oct. 16–20, 1973, S. 344. Fritz,H., Tschesche,H., Greene,L.J., Truscheit,E. (eds.), Berlin-Heidelberg-New York: Springer 1974

    Google Scholar 

  9. Wilson,K.A., Laskowski,M.,sr.: J. Biol. Chem.250, 4261 (1975)

    PubMed  Google Scholar 

  10. Krahn,J., Stevens,F.C.: Biochemistry9,2646 (1970)

    PubMed  Google Scholar 

  11. Hirs,C.H.W.: Performic acid oxidation. In: Methods in Enzymology XI, S. 197. Colowick,S.P., Kaplan,N.O. (eds.), New York: Academic Press 1967

    Google Scholar 

  12. Belitz,H.D., Fuchs,A., Nitsche,G., Al-Sultan,T.: Z. Lebensm. Unters: Forsch.150, 215 (1972)

    Google Scholar 

  13. Gray,W.R.: Sequential degradation plus dansylation. In: Methods in Enzymology XI, S. 469. Siehe (11)

    Google Scholar 

  14. Röhm GmbH (Firmenschrift): Aminopeptidase M

  15. Röhm GmbH (Firmenschrift): Aminopeptidase O

  16. Light,A.: Leucine aminopeptidase in sequence determination of peptides. In: Methods in Enzymology [11] XXV (Colowick,S.P., Kaplan,N.O. eds.), S. 253, New York: Academic Press 1972

    Google Scholar 

  17. Jolles,J., Jollès,P., Uhlig,H., Lehmann,K.: Hoppe-Seyler's Z. physiol. Chem.350, 139 (1969)

    PubMed  Google Scholar 

  18. Ambler,R.P.: Enzymic hydrolysis with carboxypeptidases. In: Methods in Enzymology XI, S. 155. Siehe (11)

    Google Scholar 

  19. Folk,J.E., Schirmer,E.W.: J. biol. Chem.238, 3884 (1963)

    PubMed  Google Scholar 

  20. Ambler,R.P.: Carboxypeptidases A and B. In: Methods in Enzymology XXV, S. 262. Siehe [16](

    Google Scholar 

  21. Light,A.: Leucine aminopeptidase (LAP). In: Methods in Enzymology XI, S. 426. Siehe

  22. Schechter,I., Berger,A.: Biochem. Biophys. Res. Commun.27, 157 (1967)

    PubMed  Google Scholar 

  23. Wilson,K.A., Laskowski,M.,sr.: The partial linear sequence of garden bean inhibitor II and location of the protease reactive sites. In: Bayer-Symposium V, S. 286. Siehe [8]

    Google Scholar 

  24. Laskowski,M.jr., Sealock,R.W.: Protein proteinase inhibitors-Molecular aspects. In: The Enzymes, Vol. III (Boyer,P.D. ed.), S. 420. New York: Academic Press 1971

    Google Scholar 

  25. Weder,J.K.P., Kassubek,A.: Z. Lebensm. Unters.-Forsch.156, 22 (1974)

    Google Scholar 

  26. Hochstrasser,K., Illchmann,K., Werle E.: Hoppe-Seyler's Z. physiol. Chem.351, 721 (1970)

    PubMed  Google Scholar 

  27. Ryan,C.A., Hass,G.M., Kuhn,R.W., Neurath,H.: Carboxypeptidase inhibitor from potatoes, properties and amino acid sequence. In: Bayer-Symposium V, S. 565. Siehe [8]

    Google Scholar 

  28. Richardson,M.: Biochem. J.137, 101 (1974)

    PubMed  Google Scholar 

  29. Richardson,M., Cossins,L.: FEBS Lett.45, 11 (1974)

    PubMed  Google Scholar 

  30. Reddy,M.N., Keim,P.S., Heinrikson,R.L., Kézdy,F.J.: J. Biol. Chem.250, 1741 (1975)

    PubMed  Google Scholar 

  31. Laskowski,M., jr., Kato,I., Leary,T.R., Schrode,J., Sealock,R.W.: Evolution of specificity of protein proteinase inhibitors. In: Bayer-Symposium V, S. 597. Siehe [8]

    Google Scholar 

  32. Ozawa,K., Laskowski,M., jr.: J. biol. Chem.241, 3955 (1966)

    PubMed  Google Scholar 

  33. Krahn,J., Stevens,F.C.: Biochemistry11, 1804 (1972)

    PubMed  Google Scholar 

  34. Seidl,D.S., Liener,I.E., Jarvis,M.A.: Biochim. Biophys. Acta251, 83 (1971)

    PubMed  Google Scholar 

  35. Seidl,D.S., Liener,I.E., Jarvis,M.A.: Biochem. Biophys. Acta258, 303 (1972)

    PubMed  Google Scholar 

  36. Belitz,H.-D., Fuchs,A.: Z. Lebensm. Unters.-Forsch.152, 129 (1973)

    Google Scholar 

  37. Iwasaki,T., Kiyohara,T., Yoshikawa,M.: J. Biochem. (Tokyo)73, 1039 (1973)

    Google Scholar 

  38. Kress,L.F., Laskowski,M.,sr.: J. biol. Chem.243, 3548 (1968)

    PubMed  Google Scholar 

  39. Cechová,D., Svestková,V., Keil,B., Sorm,F.: FEBS Lett.4, 155 (1969)

    PubMed  Google Scholar 

  40. Takahashi,H., Iwanaga,S., Kitagawa,T., Hokama,Y., Suzuki,T.: Novel proteinase inhibitors in snake venoms: Distribution, isolation, and amino acid sequence. In: Bayer-Symposium V, S. 265. Siehe [8]

    Google Scholar 

  41. Blow,D.M.: Stereochemistry of substrate binding and hydrolysis in the trypsin family of enzymes. In: Bayer-Symposium V, S. 473. Siehe [8]

    Google Scholar 

  42. Hartley,B.S.: Phil. Trans. Roy. Soc. London, Ser. B257, 77 (1970)

    Google Scholar 

Download references

Author information

Authors and Affiliations

  1. Institut für Lebensmittelchemie der Technischen Universität München, Lothstr. 17, D-8000, München 2

    Heinz-Dieter Hory & Jürgen K. P. Weder

Authors
  1. Heinz-Dieter Hory
    View author publications

    You can also search for this author in PubMed Google Scholar

  2. Jürgen K. P. Weder
    View author publications

    You can also search for this author in PubMed Google Scholar

Rights and permissions

Reprints and permissions

About this article

Cite this article

Hory, HD., Weder, J.K.P. Trypsin- und Chymotrypsin-Inhibitoren in Leguminosen. Z Lebensm Unters Forch 162, 349–356 (1976). https://doi.org/10.1007/BF01122787

Download citation

  • Received:

  • Issue Date:

  • DOI: https://doi.org/10.1007/BF01122787

Search

Navigation