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American Journal of Clinical Nutrition, Vol 26, 41-47, Copyright © 1973 by The American Society for Clinical Nutrition, Inc.

Transfer ribonucleic acid of vitamin A-deficient rats

George P. Tryfiates Ph.D.1, R. F. Krause M.D., Ph.D.1, and John K. Shuler B.S.1

1 From the Department of Biochemistry, West Virginia University Medical Center, Morgantown, West Virginia 26506

The effect of vitamin A deficiency on the chromatographic elution patterns of liver tRNA from BD-cellulose was investigated. The tRNA and aminoacyl-tRNA synthetase enzymes were prepared from the liver of normal (control) and vitamin A-deficient rats. Following deacylation, tRNA from both sources was charged with an l-[3H]-amino acid mixture using homologous and heterologous synthetase preparations. The tRNA was also charged individually with the two essential amino acids, l-[3H-methyl]methionine and l-[3H] phenylalanine, using homologous synthetase enzymes. The elution profiles of labeled aminoacyl tRNA's from BD-cellulose columns were subsequently determined.

The degree of acylation of tRNA from vitamin A-deficient rats was always greater than that of normal tRNA, regardless of the source of enzyme preparation. The elution patterns from BD-cellulose of charged tRNA showed that synthetases from deficient animals acylate certain normal tRNA species which normal enzymes seem not to acylate, and that normal synthetases also acylate distinct vitamin A-deficient tRNA species. Furthermore, the elution pattern of normal tRNAphe differed from that of deficient tRNAphe in the number of eluted peaks and in their relative elution position. Whereas, in the normal case, two tRNAmet peaks were eluted in the deficient state, only one tRNAmet peak was observed.






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Copyright © 1973 by The American Society for Nutrition