Fujii K, Tsuji M, Murota K
Neurochem Res. 1986 Oct;11(10):1439-46. doi: 10.1007/BF00966223.
A new method for the isolation of high yields of collagen from human peripheral nerve is described. A major technique adopted in the present work is sedimentation of the tissue homogenates in a sucrose density gradient. The defatted fibrous material isolated after the removal of myelin was shown to be a relatively pure collagenous substance by amino acid analysis, indicating that the removal of noncollagenous proteins, especially glycoproteins, from collagen fibrils was effectively achieved by this method. The yield of collagen at this step was more than 90% of the total collagen in peripheral nerve. Subsequent extractions with solutions of neutral saline and sodium citrate were found to give further purification of the collagenous protein. The collagens from embryonic peripheral nerves were composed of Type I and III collagens, while Type III collagen was found to be less abundant in adult peripheral nerves.
本文描述了一种从人外周神经中分离高产率胶原蛋白的新方法。本研究采用的主要技术是在蔗糖密度梯度中对组织匀浆进行沉降。去除髓磷脂后分离得到的脱脂纤维材料经氨基酸分析表明是一种相对纯的胶原物质，这表明通过该方法可有效去除胶原纤维中的非胶原蛋白，尤其是糖蛋白。此步骤中胶原蛋白的产率超过外周神经中总胶原蛋白的90%。随后用中性盐水和柠檬酸钠溶液进行提取，发现可进一步纯化胶原蛋白质。胚胎外周神经中的胶原蛋白由I型和III型胶原蛋白组成，而在成体外周神经中发现III型胶原蛋白含量较少。
