Abstract
The lag in polymerization of calf spleen profilactin in response to addition of MgCl 2 can be overcome by smail amounts of spectrin-actin-band 4.1 complex, covalently crosslinked actin oligomers or sonicated F-actin. All of these factors also nucleate polymerization of pure actin. Another nucleator of actin polymerization, villin, delays filament formation from profilactin. A simple model of the interaction of profilin with actin can explain these apparently conflicting results in terms of the polarity with which actin filaments elongate from the different nuclei.
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Schedule a callMore From: Biochimica et Biophysica Acta (BBA) - Proteins & Proteomics
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