ELEK S D, SMITH B V, HIGHMAN W
Immunology. 1964 Sep;7(5):570-85.
Flagellar fragments are thin cylinders that are particularly suitable for the study of agglutination by electron microscopy. Their shape leads to a characteristic pattern of agglutination and thus the early stages can be studied. Measurement of interflagellar distances under conditions of negative staining, suggest that the minimum length of the rabbit antibody molecules is about 180 Å. The molecules carry the specific sites at the ends of the long axis, and become attached radially to the surface of the flagella, resembling the bristles of a bottle-brush. To explain this orientation it is postulated that the antibody is inserted into the surface of the flagellum in such a manner that surrounding molecules give it a fixed direction. Geometrically this hypothesis corresponds to an insertion into pits. Pepsin-treated (5S) rabbit antibody behaves in a like manner, but the molecule appears to be shorter. No information could be obtained about the thickness and actual shape of antibody molecules by the techniques employed.
鞭毛片段是细圆柱体,特别适合通过电子显微镜研究凝集作用。它们的形状导致了一种特征性的凝集模式,因此可以研究早期阶段。在负染色条件下测量鞭毛间距离表明,兔抗体分子的最小长度约为180埃。这些分子在长轴末端带有特异性位点,并径向附着在鞭毛表面,类似于瓶刷的刷毛。为了解释这种取向,推测抗体以这样一种方式插入鞭毛表面,即周围分子给它一个固定的方向。从几何学上讲,这个假设相当于插入凹坑中。经胃蛋白酶处理的(5S)兔抗体表现出类似的行为,但分子似乎更短。通过所采用的技术无法获得关于抗体分子厚度和实际形状的信息。