Protein organization of rat synaptic plasma membranes and synaptic vesicles: a one- and two-dimensional study.
The protein organization of rat brain synaptic plasma membranes (SPM) and synaptic vesicles (SV) was investigated by surface iodination and one- and two-dimensional electrophoresis. Polypeptides of molecular weights (MWs, in Kilodaltons) 170 K, 135 K, 96-86 K, 68-64-61 K, 56 K, 52 K, 38 K, 35-33 K, and 18 K are predominantly or exclusively exposed on the extracellular side of synaptosomes. Several polypeptides of MW between 70 K and 40 K are exclusively exposed on the cytoplasmic side of SPM. The use of two-dimensional electrophoresis allowed to recognize that, for some classes of MW, there are polypeptides of nearly the same MW and different isoelectric points exposed on both sides of SPM. The synaptosomal membrane shows a predominance of acidic proteins on the extracellular side and more neutral and basic proteins on the cytoplasmic side. With respect to SPM, SV are particularly enriched with polypeptides of MW 71 K, 56 K, 39-38 K, 32 K, 16 K, and 15 K. One of them, a doublet of MW 39-38 K, is the most highly labeled species upon surface iodination and is similar, but not identical, with a doublet located on the cytoplasmic side of SPM.
D000818:Animals; D001345:Autoradiography; D002540:Cerebral Cortex / Q000032:analysis*; D004591:Electrophoresis, Polyacrylamide Gel; D007525:Isoelectric Focusing; D008565:Membrane Proteins / Q000032:analysis*; D009419:Nerve Tissue Proteins / Q000032:analysis*; D051381:Rats; D013570:Synaptic Membranes / Q000032:analysis*; D013574:Synaptosomes / Q000032:analysis
D008565:Membrane Proteins; D009419:Nerve Tissue Proteins