The elution profile of aspartyl transfer RNA (aspartyl-tRNA) from reversed phase 5 chromatography for tRNA from a spectrum of animal tissues and tumors and human tumors has been examined. It was found that SV40-induced hamster tumors, BHK21/cl 13 cells in culture, certain carcinogen-induced tumors in the Ehrlich ascites tumor, and a number of human carcinomas and adenocarcinomas contained a distinct increase (3- to 20-fold) in the percentage of a late-eluting aspartyl-tRNA over that found in nonmalignant tissues, other animal tumors, and in human melanomas and sarcomas. The ability of the late-eluting aspartyl-tRNAAspIV to bind to ribosomes in the presence of the codons for aspartic acid was compared to that of aspartyl-tRNAAspIII and was found to be approximately the same. Also, the ability of each of the 4 isoaccepting species of aspartyl-tRNA to engage in ribosomal incorporation of aspartic acid into a polypeptide was determined. All 4 isoacceptors function equally well in the amino acid incorporation.

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Supported by grants from the Robert A. Welch Foundation, Houston, Texas; the American Cancer Society; and T. K. Dixon, Jr.

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