Light N, Bailey A J
FEBS Lett. 1985 Mar 25;182(2):503-8. doi: 10.1016/0014-5793(85)80363-x.
Collagen from bone, dentine and tendon (type I), all of which contain the pyridinoline cross-link at varying levels, were each digested with CNBr. The resulting peptide mixtures were resolved by gel filtration on A1.5m agarose and assayed for pyridinoline. The polymeric cross-linked peptide complex, poly alpha 1CB6 [(1980) Biochem. J. 189, 111] isolated from each of these tissues did not contain pyridinoline. Only one peptide fraction contained the pyridinoline cross-link; that identified as alpha 2CB3,5. However, this peptide showed only a small increase in Mr in its cross-linked form (approx. 2000-5000) demonstrating that pyridinoline is not involved in the formation of polymeric structures like poly alpha 1CB6. These data, considered in the light of the recent finding that pyridinoline is present in type I collagens from different sources in widely varying amounts, cast doubt on its role in collagen maturation.
来自骨骼、牙本质和肌腱的I型胶原蛋白，它们都含有不同水平的吡啶啉交联，分别用溴化氰进行消化。所得肽混合物通过在1.5m琼脂糖上进行凝胶过滤分离，并对吡啶啉进行测定。从这些组织中分离出的聚合交联肽复合物，即聚α1CB6 [（1980年）《生物化学杂志》189卷，111页]，不含吡啶啉。只有一个肽组分含有吡啶啉交联；即鉴定为α2CB3,5的组分。然而，该肽在其交联形式下分子量仅略有增加（约2000 - 5000），表明吡啶啉不参与像聚α1CB6这样的聚合结构的形成。鉴于最近发现吡啶啉在来自不同来源的I型胶原蛋白中的含量差异很大，这些数据对其在胶原蛋白成熟中的作用提出了质疑。
