Colby R H
J Cell Biol. 1971 Dec;51(3):763-71. doi: 10.1083/jcb.51.3.763.
Patterns of intrinsic birefringence were revealed in formalin-fixed, glycerinated myofibrils from rabbit striated muscle, by perfusing them with solvents of refractive index near to that of protein, about 1.570. The patterns differ substantially from those obtained in physiological salt solutions, due to the elimination of edge- and form birefringence. Analysis of myofibrils at various stages of shortening has produced results fully consistent with the sliding filament theory of contraction. On a weight basis, the intrinsic birefringence of thick-filament protein is about 2.4 times that of thin-filament protein. Nonadditivity of thick- and thin-filament birefringence in the overlap regions of A bands may indicate an alteration of macromolecular structure due to interaction between the two types of filaments.
通过用折射率接近蛋白质的溶剂(约1.570)灌注来自兔横纹肌的福尔马林固定、甘油处理的肌原纤维,揭示了其固有双折射模式。由于消除了边缘双折射和形态双折射,这些模式与在生理盐溶液中获得的模式有很大不同。对不同缩短阶段的肌原纤维进行分析所得到的结果与收缩的滑动丝理论完全一致。以重量计,粗丝蛋白的固有双折射约为细丝蛋白的2.4倍。A带重叠区域中粗丝和细丝双折射的非加和性可能表明由于两种类型的细丝之间的相互作用而导致大分子结构的改变。