Eipert S R, Black S H
Arch Microbiol. 1979 Mar 12;120(3):205-14. doi: 10.1007/BF00423067.
The cytoplasmic fibrils of Treponema refringens were studied in situ by electron microscopy of thin sectioned and negatively stained cells. From 5 to 21 parallel fibrils ran through the cell in a band adjacent to the inner side of the cytoplasmic membrane, on the inner sides of the curves of the spirochete. The nuclear areas of cells were adjacent to the fibrils. Cross sections of fibrils isolated from cells which had been lysed were polygonal and not uniformly electron dense. Polyacrylamide gel electrophoresis of partially purified fibril preparations indicated their main component to be a protein with a molecular weight of 97,000. Fibrils were solubilized by 1% trypsin, 1% pronase, 6 M urea, 1 N HCl, 0.005 N NaOH or 1.3% sodium dodecyl sulfate. By electron microscopy of negatively stained isolated fibrils, each fibril was found to be a complex arrangement of strands rather than a single tubule.
通过对薄切片和负染细胞进行电子显微镜观察,对致密螺旋体的细胞质纤丝进行了原位研究。5至21条平行纤丝穿过细胞,位于螺旋体曲线内侧、与细胞质膜内侧相邻的一条带中。细胞的核区与纤丝相邻。从已裂解细胞中分离出的纤丝横截面呈多边形,且电子密度不均匀。对部分纯化的纤丝制剂进行聚丙烯酰胺凝胶电泳表明,其主要成分是一种分子量为97,000的蛋白质。纤丝可被1%胰蛋白酶、1%链霉蛋白酶、6M尿素、1N盐酸、0.005N氢氧化钠或1.3%十二烷基硫酸钠溶解。通过对负染的分离纤丝进行电子显微镜观察,发现每条纤丝是由多股组成的复杂结构,而非单个小管。