Introduction of New Crosslinks into Proteins

  • Klaus Ziegler
  • Irene Schmitz
  • Helmut Zahn
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 86A)


Analysis of the crosslinks ε-(γ-glutamyl) lysine and ε-(β-aspartyl) lysine present in treated wool has been improved by modifying the enzymic digestion.

Treatment of wool with either monocarboxylic acid chlorides in dimethylsulfoxide or with l-fluoro-2,4-dinitrobenzene in the presence of acetate considerably decreased ε-amino groups and solubility. Since no information of interchain amide crosslinks was observed, the hypothesis of so-called self-crosslinking postulated by ZAHN has to be withdrawn. The effects of both treatments are explained in the light of new results.

The reaction of wool with glutaraldehyde leads to a stabilization of the fiber. Experiments with glutaraldehyde and primary alkyl amines as model compounds revealed that the cyclic form of the aldehyde gave the unstable N-alkyl-2,6-dihydroxypiperidine, which either looses water to give N-alkyldihydropyridine or condenses with 2,6-dihydroxytetrahydropyran to yield a copolyether which was isolated. According to recent publications, crosslinking of proteins by glutaraldehyde is due to the formation of quaternary pyridinium compounds.


Carboxylate Anion Mixed Anhydride Pyridinium Chloride Hypothetical Scheme Aminohexanoic Acid 
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  1. Asquith, R. S. and Otterburn, M. S. (1971). Self-crosslinking in keratin under the influence of dry heat. Appl. Polymer Symp., 18, 277.Google Scholar
  2. Asquith, R. S., Otterburn, M. S., Buchana, J. H., Cole, M., Fletcher, J. C. and Gardner, K. L. (1970). The identification of ε-(γ-L-glutamyl)-L-lysine cross-links in native wool keratins. Biochim. Biophys. Acta, 221, 342.PubMedGoogle Scholar
  3. Cole, M., Fletcher, J. C., Gardner, K. L. and Corfield, M. C. (1971). A study of enzymatic hydrolysis applicable to the examination of processed wools. Appl. Polymer Symp., 18, 147.Google Scholar
  4. Di Modica, G. and Marzona, M. (1971). Cross-linking of wool keratin by bifunctional aldehydes. Text. Res. J., 41, 701.Google Scholar
  5. Happich, W. F., Windus, W. and Naghski, J. (1965). Stabilization of wool by glutaraldehyde. Text. Res. J., 35, 850.CrossRefGoogle Scholar
  6. Happich, W. F. (1971). New process expands uses for wool-skins. Appl. Polymer Symp., 18, 1483.Google Scholar
  7. Hardy, P. M., Nicholls, A. C. and Rydon, H. N. (1976a). The nature of cross-linking of proteins by glutaraldehyde. Part I. Interaction of glutaraldehyde with the amino-groups of 6-aminohexanoic acid and of α-N-acetyl-lysine. J. Chem. Soc. Perkin T.I., 9, 958.CrossRefGoogle Scholar
  8. Hardy, P. M., Graham, J. H. and Rydon, H. N. (1976b). Formation of quaternary pyridinium compounds by the action of glutaraldehyde on proteins. J. Chem. Soc. Chem. Comm., 5, 157.CrossRefGoogle Scholar
  9. Kusch, P., Lubig, R. and Topert, G. (1972). Ein neues Verfahren zur chemischen Fixierung von Krimmergarn. Melliand Textilber., 53, 1393.Google Scholar
  10. Lubig, R. (1972). Ein Beitrag zur Umsetzung von Wolle mit Glutaraldehyd. Dissertation, Technische Hochschule Aachen.Google Scholar
  11. Milligan, B., Holt, L. A. and Caldwell, J. B. (1971). The enzymic hydrolysis of wool for amino acid analysis. Appl. Polymer Symp., 18, 113.Google Scholar
  12. Reinert, F. (1972). Reaktionen des l-Fluor-2,4-dinitrobenzols mit Faserproteinen, seine Nebenreaktionen und sich daraus ergebende Eigenschaftsanderungen. Dissertation, Technische Hochschule Aachen.Google Scholar
  13. Scharff, H. D. (1972). Reaktionen von Faserproteinen mit Carbonsäurechloriden in dipolaren aprotischen Lösungsmitteln. Dissertation, Technische Hochschule Aachen.Google Scholar
  14. Schmitz, I., Baumann, H. and Zahn, H. (1976). Ein Beitrag zur enzymatischen Totalhydrolyse von Wollkeratin. Proc. Int. Wool Text. Res. Conf., Aachen 1975 II, 313.Google Scholar
  15. Schmitz, I. (1975). Analyse von saurelabilen Aminosaure-derivaten nach enzymatischer Totalhydrolyse von Proteinen und Keratinen. Dissertation, Technische Hochschule Aachen.Google Scholar
  16. Zahn, H., Beyer, H., Hammoudeh, M. M. and Schallah, A. (1969). Vernetzungs-und Selbstvernetzungsreaktionen bei Wolle. Melliand Textilber., 50, 1319.Google Scholar
  17. Zahn, H., Schallah, A., Scharff, H. D. and Meichelbeck, H. (1971). Crosslinking of wool during treatment with carboxylic acid chlorides. Appl. Polymer Synp., 18, 163.Google Scholar
  18. Ziegler, K. and Liesenfeld, I. (1976). Studies on glutaraldehyde treated wool. Proc. Int. Wool Text. Res. Conf., Aachen 1975 III, 88.Google Scholar

Copyright information

© Plenum Press, New York 1977

Authors and Affiliations

  • Klaus Ziegler
    • 1
  • Irene Schmitz
    • 1
  • Helmut Zahn
    • 1
  1. 1.Deutsches WollforschungsinstitutAachenFederal Republic of Germany

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