Jahn R, Schiebler W, Ouimet C, Greengard P
Proc Natl Acad Sci U S A. 1985 Jun;82(12):4137-41. doi: 10.1073/pnas.82.12.4137.
A protein with an apparent molecular mass of 38,000 daltons designated p38 was found in synaptic vesicles from rat brain. The subcellular distribution of p38 and some of its properties were determined with the aid of polyclonal and monoclonal antibodies. The subcellular distribution of p38 was similar to that of synapsin I, a synaptic-vesicle specific phosphoprotein. p38 in the synaptic vesicle fraction purified by controlled-pore glass bead chromatography showed an enrichment of more than 20-fold over the crude homogenate. Immunostaining of sections through various brain regions revealed an intense labeling of most, and possibly all, nerve terminals. Only faint reaction in the region of the Golgi apparatus and no detectable labeling of axons and dendrites was observed. Two-dimensional electrophoresis revealed that p38 has an acidic pI. Solubilization experiments, as well as phase separation experiments using Triton X-114, indicated that p38 is an integral membrane protein. Binding of antibodies to intact synaptic vesicles, as well as controlled proteolytic digestion of intact and detergent-treated vesicles, revealed that p38 has a domain exposed on the cytoplasmic surface.
在大鼠脑的突触小泡中发现了一种表观分子量为38,000道尔顿的蛋白质，命名为p38。借助多克隆抗体和单克隆抗体确定了p38的亚细胞分布及其一些特性。p38的亚细胞分布与突触素I（一种突触小泡特异性磷蛋白）相似。通过可控孔径玻璃珠层析纯化的突触小泡组分中的p38比粗匀浆富集了20多倍。对不同脑区切片的免疫染色显示，大多数（可能是所有）神经末梢有强烈标记。在高尔基体区域仅观察到微弱反应，未检测到轴突和树突的标记。二维电泳显示p38具有酸性pI。溶解实验以及使用Triton X-114的相分离实验表明，p38是一种整合膜蛋白。抗体与完整突触小泡的结合，以及对完整和经去污剂处理的小泡进行可控的蛋白水解消化，表明p38有一个暴露于细胞质表面的结构域。
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