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Location of the Intermolecular Crosslinking Sites in Collagen

  • Chapter
Protein Crosslinking

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

Abstract

Collagen is stabilized by intermolecular crosslinks which occur following the enzymatic conversion of the ε-amino groups of selected lysyl and hydroxylysyl residues to the aldehydes, allysine and hydroxyallysine. These aldehydes combine specifically with other allysine or hydroxyallysine residues and/or the side chains of lysine, hydroxylysine or histidine to produce characteristic crosslinks composed of two, three, or four amino acid components. These crosslinks may be converted to more complex compounds by reaction with other amino acids. The newly discovered crosslink, hydroxyaldol-histidine, appears to arise by condensation of one residue each of allysine, hydroxyallysine, and histidine. It was found in a peptide from a tryptic digest of insoluble calf skin collagen which contains three constituent chains, one arising from a region of αl-CB5 and one from αl-CB6. Data obtained in this laboratory, from peptides which were originally isolated from an extensive proteolytic digest of reconstituted calf skin collagen are consistent with a crosslink between the hydroxylysine at residue 927 in αl-CB6 and the allysine at residue 9N in αl-CB(0,1). This is supported by other investigators who have isolated an analogous crosslinked peptide from CNBr digests. The amino acid sequence of a peptide derived from limited alkaline hydrolysis of insoluble calf bone collagen indicates the presence of the crosslink S,ô’-dihydroxylysinonorleucine at residue 671 in αl-CB7. It is apparent, on both theoretical and experimental bases, that many more cross-linked peptides occur; detailed studies should elucidatethe three-dimensional structure of the collagen fibril.

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Authors and Affiliations

  1. Department of Biochemistry, University of Connecticut Health Center, Farmington, Connecticut, 06032, USA

    Norma P. Stimler & Marvin L. Tanzer

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  1. Norma P. Stimler
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  2. Marvin L. Tanzer
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Editors and Affiliations

  1. Western Regional Research Laboratory, U.S. Department of Agriculture, Agricultural Research Service, Berkeley, California, USA

    Mendel Friedman

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Stimler, N.P., Tanzer, M.L. (1977). Location of the Intermolecular Crosslinking Sites in Collagen. In: Friedman, M. (eds) Protein Crosslinking. Advances in Experimental Medicine and Biology, vol 86. Springer, Boston, MA. https://doi.org/10.1007/978-1-4757-9113-6_37

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  • DOI: https://doi.org/10.1007/978-1-4757-9113-6_37

  • Publisher Name: Springer, Boston, MA

  • Print ISBN: 978-1-4757-9115-0

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