Townsend R, Archer D B, Plaskitt K A
J Bacteriol. 1980 May;142(2):694-700. doi: 10.1128/jb.142.2.694-700.1980.
Fibrils 3.5 nm in diameter were released from the honeybee spiroplasma (BC3) by treatment with detergents and then purified by isopycnic centrifugation. Purified fibrils were flexuous, of indeterminate length, and had an axial repeat of 8.5 nm. The fibrils were associated in pairs, but in 1 M salt formed aggregates with a marked striated appearance. Pronase completely degraded the fibrils, but trypsin had little effect. The fibrils were composed of a single protein of molecular weight 55,000 which represented about 1% of the total cell protein. A protein of molecular weight 26,000 appeared to be associated with the fibrils. The significance of this in relation to membrane attachment and the possible role of fibrils in maintenance of cell shape and in motility are discussed.
通过用洗涤剂处理，从蜜蜂螺旋体（BC3）中释放出直径为3.5纳米的纤丝，然后通过等密度离心进行纯化。纯化后的纤丝呈弯曲状，长度不确定，轴向重复距离为8.5纳米。纤丝成对存在，但在1M盐溶液中会形成具有明显条纹外观的聚集体。链霉蛋白酶能完全降解纤丝，但胰蛋白酶几乎没有作用。纤丝由一种分子量为55,000的单一蛋白质组成，该蛋白质约占细胞总蛋白的1%。一种分子量为26,000的蛋白质似乎与纤丝相关。文中讨论了这与膜附着的关系以及纤丝在维持细胞形状和运动方面可能发挥的作用。
