Purification of terminal riboadenylate transferase from calf thymus gland.

@article{Tsiapalis1975PurificationOT,
  title={Purification of terminal riboadenylate transferase from calf thymus gland.},
  author={Chris Milton Tsiapalis and J W Dorson and Frederick Bollum},
  journal={The Journal of biological chemistry},
  year={1975},
  volume={250 12},
  pages={4486-96}
}
A poly(A) polymerase has been purified from the soluble protein fraction of calf thymus gland. The activity is cytoplasmic and nonparticulate. Mn-2+ATP is the preferred substrate. On the basis of disc gel electrophoresis in sodium dodecyl sulfate-acrylamide gels, gel filtration, and sedimentation velocity in sucrose gradients, the enzyme has a molecular weight of 62,000 and appears to consist of one polypeptide chain. The enzyme preparation is shown to be nearly homogeneous by disc gel… CONTINUE READING
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