Degradation of the arginyl-tRNA synthetase protein during purification by affinity chromatography on immobilized total tRNA and immobilized tRNA, specific for arginyl-tRNA synthetase.
Arginyl-tRNA synthetase was prepared from Bom:NMRI mouse liver postribosomal supernatants. Purification was performed by either gel filtration on Sephadex G-200 or chromatofocusing before affinity chromatography on immobilized total tRNA (mixture of tRNA's, specific for all aminoacyl-tRNA synthetases), followed by affinity chromatography on immobilized tRNA, specific for arginyl-tRNA synthetase. The purification factor for arginyl-tRNA synthetase activity was 16700x. Following sodium dodecyl sulphate polyacrylamide electrophoresis several protein bands were found in the purified material. All these protein bands were shown to possess arginyl-tRNA synthetase activity.
Berg
B H
BH
Department of Biochemistry and Molecular Biology, University of Bergen, Norway.
D000604:Amino Acyl-tRNA Synthetases / Q000302:isolation & purification; D000818:Animals; D001126:Arginine-tRNA Ligase / Q000302:isolation & purification* / Q000378:metabolism*; D002846:Chromatography, Affinity; D002850:Chromatography, Gel; D004591:Electrophoresis, Polyacrylamide Gel; D008099:Liver / Q000201:enzymology; D051379:Mice; D012347:RNA, Transfer, Arg
D012347:RNA, Transfer, Arg; D000604:Amino Acyl-tRNA Synthetases; D001126:Arginine-tRNA Ligase