Format

Send to

Choose Destination
Methods. 2008 May;45(1):65-74. doi: 10.1016/j.ymeth.2008.01.002.

Advances in collagen cross-link analysis.

Author information

1
Orthopaedic Research Labs, Department of Orthopaedics & Sports Medicine, University of Washington, 1959 NE Pacific Street, Seattle, WA 98195-6500, USA. deyre@u.washington.edu

Abstract

The combined application of ion-trap mass spectrometry and peptide-specific antibodies for the isolation and structural analysis of collagen cross-linking domains is illustrated with examples of results from various types of collagen with the emphasis on bone and cartilage. We highlight the potential of such methods to advance knowledge on the importance of post-translational modifications (e.g., degrees of lysine hydroxylation and glycosylation) and preferred intermolecular binding partners for telopeptide and helical cross-linking domains in regulating cross-link type and placement.

PMID:
18442706
PMCID:
PMC2398701
DOI:
10.1016/j.ymeth.2008.01.002
[Indexed for MEDLINE]
Free PMC Article

Supplemental Content

Full text links

Icon for Elsevier Science Icon for PubMed Central
Loading ...
Support Center