Abstract
Four isoacceptor species of phenylalanyl-tRNA, from rat-liver total tRNA, have been purified to homogeneity using sequential chromatography on BD-cellulose and reversed-phase-5 (RPC-5) columns. Re-chromatography of individual species (I–IV) on RPC-5 columns revealed chromatographic homogeneity (single peak, same site and height of elution) and biological homogeneity since none of the species accepted amino acids other than phenylalanine. Thermal denaturation profiles and circular dichroism spectral patterns suggested that these species exist in two major conformations.
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