Identification of hydroxypyridinium cross-linking sites in type II collagen of bovine articular cartilage.
Identification of hydroxypyridinium cross-linking sites in type II collagen of bovine articular cartilage.
复制标题
牛关节软骨 II 型胶原中羟基吡啶鎓交联位点的鉴定。
DOI：
10.1021/bi00303a041
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发表时间：
1984
期刊：
影响因子：
2.9
通讯作者：
Eyre,DR
中科院分区：
文献类型：
--
作者：
Wu,JJ;Eyre,DR
摘要：在成熟软骨中，3-羟基吡啶交联残基提供的共价分子间键增强了胶原原纤维。为了确定这些三功能交联在II型胶原分子中的位置，我们从牛关节软骨的胃蛋白酶可溶性胶原和盐酸胍不溶性胶原中分析了CNBr肽。羟基吡啶残基在胶原a链和cnbr衍生肽中的存在通过其特有的自然荧光检测。定量地说，从胃蛋白酶可溶性胶原蛋白中发现大约三分之一的a链含有羟基吡啶残基。通过CM-cellulose和Bio-Gel P-30的柱层析和十二烷基硫酸钠-聚丙烯酰胺的平板凝胶电泳，对其进行了纯化。两种pep-的组成及性质
Jiann-Jiu Wu and David R. Eyre** abstract: In mature cartilage, collagen fibrils are strengthened by covalent intermolecular bonds provided by 3-hydroxypyridinium cross-linking residues. To determine the location of these trifunctional cross-links within the type II collagen molecule, CNBr peptides were analyzed from pepsin-soluble collagen and from guanidine hydrochloride insoluble collagen of bovine articular cartilage. The presence of hy-droxypyridinium residues in collagen a chains and CNBr-derived peptides was detected by their characteristic natural fluorescence. Quantitatively, about one in three a chains from pepsin-soluble collagen was found to contain a hydroxypyridinium residue. Its distribution in the chains was limited to two CNBr peptides, which were purified by column chromatography on CM-cellulose and Bio-Gel P-30 followed by slab-gel electrophoresis in sodium dodecyl sulfate-poly-acrylamide. The composition and properties of the two pep-