Proteins and glycoproteins of rat cerebral cortex subsynaptosomal fractions: Extraction with sodium dodecylsulphate and analytic electrophoresis

Study of nerve impulse transmission has led to the development of techniques for isolation of or nerve ending particles [1-5] which retain the morphology and transmitter content of the original terminals. Recent reports have indicated that protein [6-8] ,glycoprotein [9] and glycolipid [9] synthesis occurs in synaptosomes. This laboratory [ 10] has recently demonstrated that protein, glycoprotein, lipid, and glycolipid synthesis occurs in isolated synaptosomes in vitro and that the intraneural mitochondrion is one subsynaptosomal particle independently carrying out these syntheses. Because of the occurrence of protein and glycoprotein synthesis in isolated synaptosomes it seemed of import to determine the extraction and the electrophoretic separation of the proteins of subsynaptosomal fractions and to determine which of these proteins are glycoproteins. The present communication describes such a study. Waehneldt and Mandel [ 11 ] have recently described the extraction with sodium dodecyl sulfate and electrophoresis of rat brain myelin proteins; this report gives the electrophoretic patterns of other fractions of rat brain solubilized by sodium dodecyl sulphate (SDS).