Identification of actin in highly purified synaptic vesicles from the electric organ of Torpedo marmorata.

Evidence has been obtained that actin is a major constituent of highly purified synaptic vesicles isolated from the electric organ of Torpedo marmorata. The mobility of a prominent spot in the polypeptide pattern of vesicles in high-resolution two-dimensional polyacrylamide gel electrophoresis is very similar to the mobility of the main component in the actin preparation purified from the whole electric organ by affinity chromatography on immobilized pancreatic deoxyribonuclease I. The comparison of tryptic peptide maps obtained from the putative vesicle actin and authentic actin from the electric organ, both purified by two-dimensional gel electrophoresis and labeled in situ with 125I, showed about 88% homology, thereby supporting the conclusion that the vesicle actin is indeed an actin isoform.