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Kuypers R, Tyler M, Kurth LB, et al. The molecular location of Ehrlich chromogen and pyridinoline cross-links in bovine perimysial collagen. Meat Sci. 1994;37(1):67-89doi: 10.1016/0309-1740(94)90146-5.
Kuypers, R., Tyler, M., Kurth, L. B., & Horgan, D. J. (1994). The molecular location of Ehrlich chromogen and pyridinoline cross-links in bovine perimysial collagen. Meat science, 37(1), 67-89. https://doi.org/10.1016/0309-1740(94)90146-5
Kuypers, R, et al. "The molecular location of Ehrlich chromogen and pyridinoline cross-links in bovine perimysial collagen." Meat science vol. 37,1 (1994): 67-89. doi: https://doi.org/10.1016/0309-1740(94)90146-5
Kuypers R, Tyler M, Kurth LB, Horgan DJ. The molecular location of Ehrlich chromogen and pyridinoline cross-links in bovine perimysial collagen. Meat Sci. 1994;37(1):67-89. doi: 10.1016/0309-1740(94)90146-5. PMID: 22059414.
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Meat Sci. 1994;37(1):67-89. doi: 10.1016/0309-1740(94)90146-5.

The molecular location of Ehrlich chromogen and pyridinoline cross-links in bovine perimysial collagen.

Meat science

R Kuypers, M Tyler, L B Kurth, D J Horgan

Affiliations

  1. CSIRO Division of Food Processing, Meat Research Laboratory, PO Box 12, Cannon Hill, Queensland 4170, Australia.

PMID: 22059414 DOI: 10.1016/0309-1740(94)90146-5

Abstract

Collagenous peptides containing the Ehrlich chromogen (EC), a trifunctional cross-link of proposed pyrrolic structure, were selectively isolated from a tryptic digest of bovine perimysial collagen by coupling to a diazotised support. Peptides containing pyridinoline (Pyr), another trifunctional cross-link but based on a 3-hydroxypyridinium ring, were isolated from the uncoupled material. The isolated cross-linked peptides were purified by chromatographic procedures and subsequently characterised by amino acid and sequence analyses. EC occurred in stoichiometric amounts in three-chained peptides derived from type I collagen cross-link regions. In contrast, Pyr was found in non-stoichiometric amounts in three-chained peptides where two of the chains were identified as the 76 amino-terminal residues of the α1 (III) collagen chain. The third chain in these Pyr cross-linked peptides was derived from the C-terminal helical cross-link region of either type III collagen or the corresponding region of type I collagen, with the former region predominating. These findings suggest that EC and Pyr cross-links of perimysial collagen are associated mainly with type I and type III collagen respectively.

Copyright © 1994. Published by Elsevier Ltd.

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