The purification and properties of valine tRNAs of Drosophila melanogaster.
The valine transfer ribonucleic acids of Drosophila melanogaster have been purified by column chromatography on BD-cellulose, Sepharose 6B, and RPC-5. Three major species were analyzed for base composition and coding properties. Valyl-tRNAVal3a binds strongly to ribosomes in the presence of GUA and to a lesser extent with GUU and GUG. Valyl-tRNAVal3b binds strongly in the presence of GUG and very poorly if at all with the other three triplets whereas valvyl-tRNAVal4, which contains inosine, binds strongly in the presence of GUU, GUC, and GUA and weakly with GUG.
D000818:Animals; D000926:Anticodon; D003062:Codon; D004331:Drosophila melanogaster / Q000032:analysis; D012343:RNA, Transfer / Q000032:analysis / Q000302:isolation & purification*; D012263:Ribonucleosides / Q000032:analysis; D014633:Valine
D000926:Anticodon; D003062:Codon; D012263:Ribonucleosides; D012343:RNA, Transfer; D014633:Valine