CHANGES IN CROSSLINKING DURING AGING IN BOVINE TENDON COLLAGEN
CHANGES IN CROSSLINKING DURING AGING IN BOVINE TENDON COLLAGEN
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DOI：
10.1016/0014-5793(79)80080-0
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发表时间：
1979-01-01
期刊：
影响因子：
3.5
通讯作者：
BAILEY, AJ
中科院分区：
文献类型：
--
作者：
LIGHT, ND;BAILEY, AJ
早期对胶原交联肽的研究主要依赖于从溴化氰消化物或硼氢化还原胶原中提取肽的色谱制备（复习[1 -3]）。伴随而来的多肽同质性的保证以及对多肽片段的正确鉴定和分析评价等问题阻碍了许多工作，但从四分之一交错重叠模型[4]推导出的交联多肽得到了相当大的支持证据。虽然很少有确凿的证据被阐明，但工作m[5-71]已经确定了n端肽在交叉收缩形成中的作用，以及c端肽的运动。螺旋-螺旋分子间交叉缩合的存在也被提出。研究表明，在与牙齿一起工作的硬组织胶原蛋白中存在这种互影响因子的可能性[9,101]。这些分析是冗长而耗时的，通常不允许比较来自不同来源或年龄组的I型胶原的交联，也没有对N-， c -端和螺旋-螺旋相互作用的相对重要性进行研究。我们已经描述了[1 1]一种快速的方法，即十二烷基硫酸钠(SDS)-聚丙烯酰胺凝胶电泳，用于直接比较和定量胶原蛋白中的交缩肽。利用这种技术结合胶原蛋白肽的特定标记，我们现在报告了在牛膝肌腱胶原蛋白成熟过程中可能导致的显著分子变化
Earlier studies on crosslinked peptides m collagen have relied predommantly on the chromatographic preparation of peptides from cyanogen bromide digests of msoluble or borohydnde reduced collagen (revrewed [l-3]). The attendant problems of assurance of peptrde homogenerty and correct rdenttfication and analytical assessment of pepttde fragments have hampered much of the work but considerable supportwe evtdence for the crosslinked peptrdes deduced from the quarter-stagger overlap model [4] has been obtained. Although little conclusive evidence has been elucidated, the work m [5-71 has estabhshed the role of N-termmal peptides m crosshnk formation and that 111 [8] the mvolvement of C-termmal peptrdes. The existence of helical-helical intermolecular crosshnks has also been proposed. The possibility of such mteractrons in hard tissue collagen from work wrth dentme has been indicated] 9,101.These analyses are tedious and trme-consummg and generally have not permitted the comparrson of crosslinkmg m type I collagen from various sources or age groups nor has a study of the relative rmportance of N-, C-terminal and helix-helix mteractions been undertaken. We have described [1 I] a rapid method, utrhsmg sodium dodecyl sulphate (SDS)-polyacrylamrde gel electrophoresis, for the direct comparrson and quantitatron of crosshnking peptrdes in collagen. Usmg thus technique combined with specific labellmg of collagen peptrdes we now report significant molecular changes during the maturatron of bovme tendon collagen that could account for