Mummery R, Sessay A, Lai F A, Beesley P W
Division of Biochemistry, School of Biological Sciences, University of London, Egham, Surrey, England.
J Neurochem. 1996 Jun;66(6):2455-9. doi: 10.1046/j.1471-4159.1996.66062455.x.
The distribution of a glycoprotein component of the muscle dystrophin complex, beta-dystroglycan, has been determined in subcellular fractions of adult rat forebrain. The results show that beta-dystroglycan is enriched in several membrane fractions, including synaptic membranes, but in marked contrast to dystrophin is not detectable in the postsynaptic density fraction. The antiserum also recognises a second molecular species of apparent molecular mass of 164 kDa which is highly enriched in the postsynaptic density fraction. Preabsorption of the antiserum with the antigen (a 22-mer peptide corresponding to the C-terminal sequence of rabbit skeletal muscle beta-dystroglycan) abolished reactivity against both beta-dystroglycan and the 164-kDa postsynaptic density-enriched protein, confirming that the two species are immunologically related. Enzymatic removal of N-linked oligosaccharide lowered the apparent molecular mass of beta-dystroglycan by 3 kDa but did not alter the mass of the 164-kDa species.
已在成年大鼠前脑的亚细胞组分中确定了肌肉肌营养不良蛋白复合物的一种糖蛋白成分β-肌营养不良聚糖的分布。结果表明,β-肌营养不良聚糖在包括突触膜在内的几个膜组分中富集,但与肌营养不良蛋白形成鲜明对比的是,在突触后致密组分中无法检测到。该抗血清还识别出另一种表观分子量为164 kDa的分子,其在突触后致密组分中高度富集。用抗原(对应于兔骨骼肌β-肌营养不良聚糖C末端序列的22肽)预吸收抗血清消除了对β-肌营养不良聚糖和164 kDa突触后致密富集蛋白的反应性,证实这两种分子在免疫上相关。酶促去除N-连接寡糖使β-肌营养不良聚糖的表观分子量降低了3 kDa,但未改变164 kDa分子的质量。