Abstract
Human erythrocyte actin can be extracted from membrane ghosts by low ionic strength treatment in the presence of protective amounts of calcium and ATP. Purification then involves a single chromatographic step. The erythrocyte actin can be labelled with N-(1-pyrenyl)iodoacetamide. The fluorescence enhancement which accompanies polymerisation can be used to determine the critical concentration for assembly and to follow the polymerisation reaction time-course. The polymerisation kinetics of erythrocyte actin are compared with those of rabbit skeletal muscle actin. The two are shown to be markedly different.
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