Abstract
A detailed analysis of the ribosomal components of chloramphenicol ribonucleic acid has revealed slight but definite differences from normal ribosomal ribonucleic acid. Both the 16 s and the 23 s components of chloramphenicol ribonucleic acid sedimented slightly faster through sucrose gradients, and had slightly less affinity for columns of methylated albumin-coated kieselguhr, than their normal counterparts. These differences are explainable in terms of secondary structure; chloramphenicol ribosomal ribonucleic acid may have a greater degree of ordered helical configuration than normal ribosomal ribonucleic acid.
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