Glattauer V, Ramshaw J A, Tebb T A, Werkmeister J A
CSIRO, Division of Biomolecular Engineering, Parkvile, Victoria, Australia.
Int J Biol Macromol. 1991 Jun;13(3):140-6. doi: 10.1016/0141-8130(91)90038-v.
The antigenic response to the helical domain of collagens is normally very low, with the nature of the epitopes recognized by antibodies being dependent on the species of origin. Thus, in certain species, for example rabbit, sequential determinants on single alpha-chains are found, whereas in other species such as mouse, conformational epitopes are predominant. A variety of techniques for identification of epitopes, including rotary shadowing, examination of specific fragments and chemical modification reactions are discussed. The application of these techniques is illustrated using a range of monoclonal antibodies to interstitial collagens. These antibodies show that epitopes are distributed over the length of the collagen molecule.
对胶原蛋白螺旋结构域的抗原反应通常非常低,抗体识别的表位性质取决于来源物种。因此,在某些物种中,例如兔子,可发现单条α链上的连续决定簇,而在其他物种如小鼠中,构象表位占主导。本文讨论了多种鉴定表位的技术,包括旋转阴影法、特定片段检测和化学修饰反应。使用一系列针对间质胶原蛋白的单克隆抗体说明了这些技术的应用。这些抗体表明表位分布在胶原蛋白分子的整个长度上。