Mechanism of action of a 16-membered macrolide. Characteristics of Dihydrorosaramicin binding to Escherichia coli ribosome and the effects of some competitors.

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Abstract
The macrolide [3H]dihydrorosaramicin binds specifically to 50S and 70S bacterial ribosomal particles. The influence of salts, pH and additives on the interaction were studied and it was found that the optimum requirement for salts was 10 mM tris-HCl (pH 7.6), 6 mM MgCl2, 60 mM NH4Cl and that .beta.-mercaptoethanol, which reacts on rosaramicin, and its dihydro derivative cannot be used. The parameters of the binding were not dependent on the technique used, i.e., equilibrium dialysis, ethanol precipitation or 2-phase partitioning. In the search for effectors of this binding, it was found that it is inhibited by other macrolides, little affected by tobramycin and chloramphenicol, and enhanced by puromycin.