Recognition of various arginine transfer ribonucleic acids with arginyl-tRNA synthetase purified from human placenta.
Arginyl-tRNA synthetase has been purified approximately 550 fold from crude extract of human placenta by the following purification steps: Ammonium sulfate fractionation, chromatographies of DEAE-cellulose and CM-Sephadex and Sephadex G-100 gel filtration. Final preparation of this enzyme has specific activity of 123 nmole of arginyl-tRNA formed per mg of protein and was free from other aminoacyl-tRNA synthetase activities. Recognition of various arginine tRNAs with this enzyme was studied using kinetic analysis of arginylation of arginine tRNA and also arginine tRNA dependent ATP-PPi exchange reaction. Affinity of this enzyme with arginine tRNA was determine from Vmas/Km values and it was in the order of rabbit, Chum salmon, B. subtilis, E. coli and yeast in both systems.
D000604:Amino Acyl-tRNA Synthetases / Q000378:metabolism*; D000818:Animals; D001120:Arginine; D001126:Arginine-tRNA Ligase / Q000302:isolation & purification / Q000378:metabolism*; D005260:Female; D006801:Humans; D007700:Kinetics; D008099:Liver; D010920:Placenta / Q000201:enzymology*; D011247:Pregnancy; D012343:RNA, Transfer; D012474:Salmon
D012343:RNA, Transfer; D001120:Arginine; D000604:Amino Acyl-tRNA Synthetases; D001126:Arginine-tRNA Ligase