Journal
METHODS
Volume 45, Issue 1, Pages 65-74Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.ymeth.2008.01.002
Keywords
collagen; cross-links; hydroxylysine; pyridinoline; lysyl oxidase; mass spectrometry
Funding
- NIAMS NIH HHS [AR 37318, R01 AR037318-21, R01 AR036794, R01 AR037318, R37 AR037318, R01 AR036794-21, R01 AR036794-20, R01 AR037318-20, R37 AR036794, R01 AR037318-21S1, R01 AR036794-22, AR 36794, R01 AR037318-19, R01 AR036794-19A1] Funding Source: Medline
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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. (C) 2008 Elsevier Inc. All rights reserved.
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