Ayad S, Kwan A P, Grant M E
FEBS Lett. 1987 Aug 10;220(1):181-6. doi: 10.1016/0014-5793(87)80899-2.
Sequential extraction of bovine growth-plate cartilage with 4 M guanidinium chloride and pepsin was used to identify the intact and pepsinized forms respectively of type X collagen. This collagen occurs predominantly as the processed [alpha 1(X)]3 form in vivo, although the procollagen [pro alpha 1(X)]3 form can also be detected. The bovine pro alpha 1(X) and alpha 1(X) chains have Mr values identical to the corresponding chick species (Mr 59,000 and 49,000). However, the pepsinized alpha 1(X)p chains (Mr 47,000) are larger than those of the chick (Mr 45,000), and the bovine collagen type X is further distinguished by being disulphide-bonded within the triple-helical domain.
用4M氯化胍和胃蛋白酶对牛生长板软骨进行顺序提取，分别鉴定X型胶原蛋白的完整形式和经胃蛋白酶处理后的形式。这种胶原蛋白在体内主要以加工后的[α1(X)]3形式存在，不过也能检测到前胶原蛋白[proα1(X)]3形式。牛的proα1(X)链和α1(X)链的分子量与相应的鸡的链相同（分子量分别为59,000和49,000）。然而，经胃蛋白酶处理后的α1(X)p链（分子量47,000）比鸡的链（分子量45,000）大，而且牛X型胶原蛋白的进一步特征是在三螺旋结构域内存在二硫键。
