Prothymosin alpha: isolation and properties of the major immunoreactive form of thymosin alpha 1 in rat thymus.

@article{Haritos1984ProthymosinAI,
  title={Prothymosin alpha: isolation and properties of the major immunoreactive form of thymosin alpha 1 in rat thymus.},
  author={A. A. Haritos and Gregory J. Goodall and Bernard L. Horecker},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={1984},
  volume={81 4},
  pages={1008-11}
}
A polypeptide containing approximately equal to 112 amino acid residues, with the thymosin alpha 1 sequence at its NH2 terminus, has been isolated from rat thymus by using a radioimmunoassay with an antibody prepared against synthetic thymosin alpha 1. The new polypeptide, named "prothymosin alpha," was found to be the major substance crossreacting with thymosin alpha 1 antiserum in rat thymus extracts; peptides corresponding to thymosin alpha 1 or thymosin alpha 11 were not detected. In gel… CONTINUE READING

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