Comparative characterization of four purified lysine-specific transfer ribonucleic acids from chicken embryos.
Four purified tRNALys species from 13-day-old chick embryo muscle have been characterized with respect to the following properties: qualitative oligoribonucleotide composition (polyacrylamide gel electrophoresis after RNase T1 digestion), anticodon response towards AAG and AAA (equilibrium dialysis and polylysine synthesis), strength of the aminoacyl bond (de-esterification kinetics), sedimentation coefficient, and temperature-dependent double helix-to-coil transition. The results confirm the existence of four molecularly independent lysine-specific tRNA's in this eukaryotic system.
D000818:Animals; D002642:Chick Embryo; D003062:Codon; D007700:Kinetics; D008239:Lysine; D008970:Molecular Weight; D009690:Nucleic Acid Conformation; D009691:Nucleic Acid Denaturation; D009843:Oligoribonucleotides / Q000032:analysis; D012343:RNA, Transfer / Q000302:isolation & purification; D006163:Ribonuclease T1; D013696:Temperature
D003062:Codon; D009843:Oligoribonucleotides; D012343:RNA, Transfer; D006163:Ribonuclease T1; D008239:Lysine