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Introduction of New Crosslinks into Proteins

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Protein Crosslinking

Part of the book series: Advances in Experimental Medicine and Biology ((AEMB,volume 86A))

Abstract

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of interchain amide crosslinks was observed, the hypothesis of so-called self-crosslinking postulated by ZAHN has to be withdrawn.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.

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© 1977 Plenum Press, New York

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Ziegler, K., Schmitz, I., Zahn, H. (1977). Introduction of New Crosslinks into Proteins. In: Friedman, M. (eds) Protein Crosslinking. Advances in Experimental Medicine and Biology, vol 86A. Springer, Boston, MA. https://doi.org/10.1007/978-1-4684-3282-4_21

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  • DOI: https://doi.org/10.1007/978-1-4684-3282-4_21

  • Publisher Name: Springer, Boston, MA

  • Print ISBN: 978-1-4684-3284-8

  • Online ISBN: 978-1-4684-3282-4

  • eBook Packages: Springer Book Archive

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