Newcombe J, Woodroofe M N, Cuzner M L
J Neurochem. 1986 Dec;47(6):1713-9. doi: 10.1111/j.1471-4159.1986.tb13079.x.
Glial fibrillary acidic protein (GFAP) in gliosed white matter from multiple sclerosis plaques and cerebral infarcts was examined by polyacrylamide gel electrophoresis and immunoblotting. Using a monoclonal antibody raised against human GFAP, up to 11 GFAP polypeptide bands of molecular weight 37-49 kilodaltons were identified in particulate and supernatant fractions of CNS tissue homogenates. Soluble GFAP constituted about one-quarter of the total GFAP in normal cerebral white matter. In brain lesions in which reactive astrocytes were observed microscopically, the proportion of soluble GFAP was increased, with a greater representation of the lower-molecular-weight forms. In brain chronic sclerotic plaques, almost all of the GFAP was in the particulate form. Purified particulate GFAP was susceptible to proteolysis at acid but not at neutral pH in the presence of CNS homogenates. In tissue autolysis studies, GFAP was stable in situ for periods well in excess of average CNS postmortem times.
采用聚丙烯酰胺凝胶电泳和免疫印迹法检测了多发性硬化斑块和脑梗死灶胶质化白质中的胶质纤维酸性蛋白（GFAP）。使用针对人GFAP产生的单克隆抗体，在中枢神经系统组织匀浆的颗粒和上清组分中鉴定出多达11条分子量为37 - 49千道尔顿的GFAP多肽条带。可溶性GFAP约占正常脑白质中总GFAP的四分之一。在显微镜下观察到反应性星形胶质细胞的脑损伤中，可溶性GFAP的比例增加，低分子量形式的GFAP占比更大。在脑慢性硬化斑块中，几乎所有的GFAP都是颗粒形式。在中枢神经系统匀浆存在的情况下，纯化的颗粒性GFAP在酸性条件下易被蛋白水解，但在中性pH条件下不易被水解。在组织自溶研究中，GFAP在原位的稳定性远远超过中枢神经系统的平均死后时间。
