Abstract
A multi-enzyme complex of mammalian aminoacyl-tRNA synthetases was isolated from rabbit reticulocytes, and purified by polyethylene glycol fractionation and gel filtration on Biogel A15m and affinity chromatography on tRNA-Sepharose. The synthetase complex contains nine synthetase activities, and the corresponding proteins as analyzed by SDS polyacrylamide gel electrophoresis. Three of the proteins showed the identical subunit molecular weights to those of the reticulocyte's elongation factor eEF1H. The eEF1α protein could not be removed by second tRNA-Sepharose column chromatography, or gel filtration on Biogel A5m or Biogel A15m. Antibodies against eEF1α react with the purified synthetase complex on the basis of dot blot analysis. This finding should provide new clues for elucidating the structural organization of the mammalian protein biosynthetic machinery.
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a call
