Liem R
J Neurochem. 1982 Jan;38(1):142-50. doi: 10.1111/j.1471-4159.1982.tb10865.x.
Neurofilaments (NF) and glial filaments (GF) were purified from bovine brain by the axonal flotation method, followed by hydroxylapatite chromatography in 8 M-urea. The proteins were shown to be competent to reassemble into intermediate filaments with removal of the denaturant, and reassembly was used as the final step in the purification of the filament proteins. The reassembly was found to be dependent on ionic strength and pH. This dependence was greater for neurofilaments than for the glial filaments. The NF and GF preparations were found not to be contaminated with each other by their gel electrophoretic profile and their immunological distinctness. The filament proteins can be obtained in high yield, and remain in solution if the urea is removed by dialysis against a low-ionic-strength buffer. Hence, they can provide a source for further biochemical studies.
通过轴突浮选法从牛脑中纯化神经丝（NF）和神经胶质丝（GF），随后在8M尿素中进行羟基磷灰石层析。结果表明，去除变性剂后，这些蛋白质能够重新组装成中间丝，并且重新组装用作丝蛋白纯化的最后一步。发现重新组装依赖于离子强度和pH值。神经丝对这种依赖性的程度大于神经胶质丝。通过凝胶电泳图谱和免疫特异性发现，NF和GF制剂没有相互污染。如果通过用低离子强度缓冲液透析去除尿素，丝蛋白可以高产率获得并保留在溶液中。因此，它们可为进一步的生化研究提供来源。
