从人脑中分离并鉴定神经胶质丝。
Isolation and characterization of glial filaments from human brain.
作者信息
Goldman J E, Schaumburg H H, Norton W T
出版信息
J Cell Biol. 1978 Aug;78(2):426-40. doi: 10.1083/jcb.78.2.426.
Abstract
Intermediate (8--9 nm) filaments of human central nervous system astrocytes were isolated from the gliosed white matter of cases of adrenoleukodystrophy (ALD). This hereditary lipidosis is characterized pathologically by demyelination, loss of axons, and replacement of the white matter of the caudal cerebrum by a glial scar. Glial filaments were composed largely of a single protein component with a mol wt of about 49,000 daltons. Smaller components (44,000--39,000 daltons) were detected in some samples, and appear to represent degradation products of the filament protein. Human neurofilaments were isolated from the normal frontal white matter of ALD cases by the standard myelin-free axon technique. Isolated glial and neurofilament proteins comigrated during acrylamide gel electrophoresis in SDS. Polypeptides resulting from cyanogen bromide cleavage of the two filament proteins were the same. Both proteins reacted with rabbit antisera raised against isolated bovine neurofilament protein and human glial fibrillary acidic protein.
摘要
从肾上腺脑白质营养不良（ALD）病例的胶质化白质中分离出人类中枢神经系统星形胶质细胞的中间丝（8 - 9纳米）。这种遗传性脂质沉积病的病理特征是脱髓鞘、轴突丧失以及大脑尾部白质被胶质瘢痕替代。胶质丝主要由一种分子量约为49,000道尔顿的单一蛋白质成分组成。在一些样本中检测到较小的成分（44,000 - 39,000道尔顿），似乎代表丝状蛋白的降解产物。通过标准的无髓鞘轴突技术从ALD病例的正常额叶白质中分离出人类神经丝。在SDS聚丙烯酰胺凝胶电泳过程中，分离出的胶质和神经丝蛋白迁移率相同。两种丝状蛋白经溴化氰裂解产生的多肽相同。两种蛋白都与针对分离出的牛神经丝蛋白和人类胶质纤维酸性蛋白产生的兔抗血清发生反应。
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