Dieringer H, Hollister D W, Glanville R W, Sakai L Y, Kühn K
Biochem J. 1985 Apr 1;227(1):217-22. doi: 10.1042/bj2270217.
A monoclonal antibody monospecific for human type IV collagen was used as a structural probe to examine aspects of the macromolecular organization of basement-membrane collagen. Electron-microscopic observation of rotary-shadowed antigen-antibody complexes demonstrated a unique binding site for the antibody 55 +/- 6 nm distant from the 7S cross-linking region of tetrameric type IV collagen. This observation allowed a series of studies that showed: (1) the localization of an intramolecular disulphide bridge within the helical domain of the molecule, (2) the alignment of major peptic-digest fragments of the alpha 1 (IV) chain, and (3) confirmation of the postulated antiparallel arrangement of individual molecules within type IV collagen tetramers.
一种对人IV型胶原具有单特异性的单克隆抗体被用作结构探针，以研究基底膜胶原大分子组织的各个方面。对旋转阴影抗原-抗体复合物的电子显微镜观察表明，抗体有一个独特的结合位点，距离四聚体IV型胶原的7S交联区域55±6nm。这一观察结果促成了一系列研究，这些研究表明：（1）分子螺旋结构域内分子内二硫键的定位；（2）α1（IV）链主要胃蛋白酶消化片段的排列；（3）证实了IV型胶原四聚体内单个分子假定的反平行排列。
