胶原交联分析的进展
Advances in collagen cross-link analysis.
作者信息
Eyre David R, Weis Mary Ann, Wu Jiann-Jiu
机构信息
Orthopaedic Research Labs, Department of Orthopaedics & Sports Medicine, University of Washington, 1959 NE Pacific Street, Seattle, WA 98195-6500, USA.
出版信息
Methods. 2008 May;45(1):65-74. doi: 10.1016/j.ymeth.2008.01.002.
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.
摘要
以各种类型胶原蛋白（重点是骨骼和软骨）的结果示例，说明了离子阱质谱法和肽特异性抗体在胶原蛋白交联域分离和结构分析中的联合应用。我们强调了此类方法在推进有关翻译后修饰（例如赖氨酸羟基化和糖基化程度）以及端肽和螺旋交联域在调节交联类型和位置方面的优选分子间结合伙伴重要性的知识方面的潜力。
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