Identification of the iodine-sensitive tyrosines in porcine pepsin.

@article{Mains1973IdentificationOT,
  title={Identification of the iodine-sensitive tyrosines in porcine pepsin.},
  author={G Mains and R H Burchell and Thomas Prof. Dr. Hofmann},
  journal={Biochemical and biophysical research communications},
  year={1973},
  volume={54 1},
  pages={
          275-82
        }
}
Porcine pepsin was iodinated at pH 6.0 and 37° with a 13-fold molar excess of [125I]triiodide. Loss of proteolytic activity levelled off at 75 ± 5%, and 2.8 ± 0.1 gram atoms of iodine were incorporated per mole of enzyme. Pepsin, iodinated in this manner, was digested with chymotrypsin. The bulk of the label was located in two peptides with the sequences: Leu-Gly-Gly-Ile-Asp-Ser-Ser-diiodoTyr-Tyr and Ile-Gly-Asp-Glu-Pro-Leu-Asn-iodoTyr. The latter peptide is the N-terminal sequence of pepsin… CONTINUE READING

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