Reese C A, Wiedemann H, Kühn K, Mayne R
Biochemistry. 1982 Mar 2;21(5):826-30. doi: 10.1021/bi00534a002.
Recently, we have isolated a new collagenous molecule from chicken hyaline cartilage after limited pepsin digestion. This molecule, which contains interchain disulfide bonds, has been called the high molecular weight fraction or HMW [Reese, C. A., & Mayne, R. (1981) Biochemistry 20, 5443-5448]. We now present a detailed model for the structure of HMW, the model being derived from analyses both of components of HMW obtained after denaturation either with or without reduction and from electron microscopic observation of replicas of HMW obtained after rotary shadowing. We propose that HMW is a typical, triple-helical collagen molecule of length 134 nm, in which one of the chains has been cleaved at a distance of 96 nm from one end of the triple helix, while the other two chains remain uncleaved. The result of this cleavage is the appearance of a recognizable kink in molecules of HMW when visualized after rotary shadowing.
最近，我们在对鸡透明软骨进行有限的胃蛋白酶消化后，分离出了一种新的胶原分子。这种分子含有链间二硫键，被称为高分子量组分或HMW[里斯，C.A.，&梅恩，R.（1981年）《生物化学》20，5443 - 5448]。我们现在提出一个关于HMW结构的详细模型，该模型是通过对变性后（无论有无还原）获得的HMW组分进行分析以及对旋转投影后获得的HMW复制品进行电子显微镜观察推导出来的。我们认为HMW是一个典型的三螺旋胶原分子，长度为134纳米，其中一条链在距三螺旋一端96纳米处被切断，而另外两条链未被切断。这种切割的结果是，在旋转投影后观察时，HMW分子中会出现一个可识别的扭结。
