Báo cáo khoa học: Vibrio cholerae hemolysin Implication of amphiphilicity and lipid-induced conformational change for its pore-forming activity
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Vibrio choleraehemolysin (HlyA), a water-soluble protein with a native monomeric relative molecular mass of 65 000, forms transmembrane pentameric channels in target bio-membranes.TheHlyAbinds to lipid vesicles nonspecifically and without saturation; however, self-assembly is triggered specifically by cholesterol.Here we show that the HlyA partitioned quantitatively to amphiphilic media irrespective of their compositions, indicating that the toxin had an amphiphilic surface.
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