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- W2016096700 abstract "Actin was dissociated from the cytoplasmic surface of the plasma membrane from Dictyosteliumdiscoideum. The cytoplasmic surface was selectively exposed by isolating the membrane by a new method using cationic beads. When purified actin was added back to the membrane the amount that bound was proportional to the actin concentration. Trypsinization of the cytoplasmic surface abolished binding while chymotrypsin was only partly effective. Far more F-actin bound to the membrane than G-actin and the binding was not inhibited by cytochalasin B. The results support the hypothesis that actin specifically interacts with unique proteins exposed on the cytoplasmic surface of the plasma membrane." @default.
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- W2016096700 date "1980-12-01" @default.
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- W2016096700 title "Actin binding to the cytoplasmic surface of the plasma membrane isolated from Dictyosteliumdiscoideum" @default.
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- W2016096700 doi "https://doi.org/10.1016/s0006-291x(80)80034-9" @default.
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