Studies with a homogeneous enzyme from rabbit erythrocytes catalyzing the insertion of guanine into tRNA.

@article{Howes1978StudiesWA,
  title={Studies with a homogeneous enzyme from rabbit erythrocytes catalyzing the insertion of guanine into tRNA.},
  author={N K Howes and Wolfgang Farkas},
  journal={The Journal of biological chemistry},
  year={1978},
  volume={253 24},
  pages={9082-7}
}
An enzyme that catalyzes a post-transcriptional modification of tRNA, resulting in replacement of a base from tRNA by guanine, has been purified 2600-fold from rabbit erythrocyte cytosol. The purest preparation migrates as a single protein band on polycrylamide gel electrophoresis and the enzymatic activity co-electrophoreses with this protein. The native enzyme has a molecular weight of 104,000 and is dissociated into two subunits of Mr= 60,000 and 43,000. The Km for guanine is 1.5 x 10(-7) M… CONTINUE READING