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Cross-linking connectivity in bone collagen fibrils: the COOH-terminal locus of free aldehydeQuantitative analyses of the chemical state of the 16c residue of the alpha 1 chain of bone collagen were performed on samples from fetal (4-6-month embryo) and mature (2-3 year old) bovine animals. All of this residue could be accounted for in terms of three chemical states, in relative amounts which depended upon the age of the animal. Most of the residue was incorporated into either bifunctional or trifunctional cross-links. Some of it, however, was present as free aldehyde, and the content increased with maturation. This was established by isolating and characterizing the aldehyde-containing peptides generated by tryptic digestion of NaB3H4-reduced mature bone collagen. We have concluded that the connectivity of COOH-terminal cross-linking in bone collagen fibrils changes with maturation in the following way: at first, each 16c residue in each of the two alpha 1 chains of the collagen molecule is incorporated into a sheet-like pattern of intermolecular iminium cross-links, which stabilizes the young, nonmineralized fibril as a whole. In time, some of these labile cross-links maturate into pyridinoline while others dissociate back to their precursor form. The latter is likely due to changes in the molecular packing brought about by the mineralization of the collagen fibrils. The resultant reduction in cross-linking connectivity may provide a mechanism for enhancing certain mechanical characteristics of the skeleton of a mature animal.
Document ID
20050000798
Acquisition Source
Legacy CDMS
Document Type
Reprint (Version printed in journal)
External Source(s)
Authors
Otsubo, K.
(Dental Research Center, University of North Carolina Chapel Hill 27514)
Katz, E. P.
Mechanic, G. L.
Yamauchi, M.
Date Acquired
August 22, 2013
Publication Date
January 21, 1992
Publication Information
Publication: Biochemistry
Volume: 31
Issue: 2
ISSN: 0006-2960
Subject Category
Life Sciences (General)
Funding Number(s)
CONTRACT_GRANT: DE08611
CONTRACT_GRANT: DE00233
CONTRACT_GRANT: DE08522
Distribution Limits
Public
Copyright
Other
Keywords
NASA Discipline Musculoskeletal
Non-NASA Center

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