Abstract
Using [3H]-Valinomycin we show here that two types of sites can be described for this cyclic depsipeptide. A first type is sensitive to low concentration of trypsin while the other, more internal, is uncovered by the use of the protease. Of these two kinds of sites, the more external one seems more concerned with the effect that Valinomycin has on protein synthesis in rabbit reticulocytes. However, when a high concentration of Valinomycin is used, all the sites can be occupied even those which can be revealed only by tripsinization. In this case, even prolonged trypsin action does not result in release of the protein synthesis inhibitory action of Valinomycin. It is concluded that hydrophobic sites are occupied by Valinomycin only after the cell surface has been saturated by hydrophylic bonds with the antibiotic.
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