The covalent modification of E. coli arginyl-tRNA synthetase by the 2',3'-dialdehydederivative of tRNA^(Arg) (tRNA_(ox)^(Arg)) resulted in the complete inactivation of the ATP-PPi ex-change and aminoacylation ...The covalent modification of E. coli arginyl-tRNA synthetase by the 2',3'-dialdehydederivative of tRNA^(Arg) (tRNA_(ox)^(Arg)) resulted in the complete inactivation of the ATP-PPi ex-change and aminoacylation activities of the enzyme. Sodium dodecyl sulfate polyacrylamide gelelectrophoresis of the ArgRS-tRNA_(ox)^(Arg) covalent complexes indicated that two bands simulta-neously appeared on the gel parallel with inactivation corresponding to different higher mo-lecular weights. This result was different from that of the other aminoacyl-tRNA synthetaselabeling systems as previously reported. Upon the ribonuclease treatment of the modifiedArgRS, less than 15% of both the initial ATP-PPi exchange and aminocylation activities wererecovered. During the whole process of labeling and RNase treatment, the two activities ofthe enzyme were closely associated.展开更多
G protein-coupled receptors(GPCRs)are involved in the control of every aspect of our behavior and physiology.GPCR can be involved in pathological processes as well and are linked to numerous diseases,including cardiov...G protein-coupled receptors(GPCRs)are involved in the control of every aspect of our behavior and physiology.GPCR can be involved in pathological processes as well and are linked to numerous diseases,including cardiovascular and mental disorders,retinal degeneration,cancer,and AIDS.This article reviews the methods of approaching photo-affinity labeling strategy to obtain the possible G protein-coupled receptors’s binding site.展开更多
基金Project supported by the National Natural Science Foundation of China.
文摘The covalent modification of E. coli arginyl-tRNA synthetase by the 2',3'-dialdehydederivative of tRNA^(Arg) (tRNA_(ox)^(Arg)) resulted in the complete inactivation of the ATP-PPi ex-change and aminoacylation activities of the enzyme. Sodium dodecyl sulfate polyacrylamide gelelectrophoresis of the ArgRS-tRNA_(ox)^(Arg) covalent complexes indicated that two bands simulta-neously appeared on the gel parallel with inactivation corresponding to different higher mo-lecular weights. This result was different from that of the other aminoacyl-tRNA synthetaselabeling systems as previously reported. Upon the ribonuclease treatment of the modifiedArgRS, less than 15% of both the initial ATP-PPi exchange and aminocylation activities wererecovered. During the whole process of labeling and RNase treatment, the two activities ofthe enzyme were closely associated.
文摘G protein-coupled receptors(GPCRs)are involved in the control of every aspect of our behavior and physiology.GPCR can be involved in pathological processes as well and are linked to numerous diseases,including cardiovascular and mental disorders,retinal degeneration,cancer,and AIDS.This article reviews the methods of approaching photo-affinity labeling strategy to obtain the possible G protein-coupled receptors’s binding site.
