Radioiodination of proteins in single polyacrylamide gel slices. Tryptic peptide analysis of all the major members of complex multicomponent systems using microgram quantities of total protein.

@article{Elder1977RadioiodinationOP,
  title={Radioiodination of proteins in single polyacrylamide gel slices. Tryptic peptide analysis of all the major members of complex multicomponent systems using microgram quantities of total protein.},
  author={John H. Elder and R A Pickett and Jacqueline Hampton and Richard Allen Lerner},
  journal={The Journal of biological chemistry},
  year={1977},
  volume={252 18},
  pages={6510-5}
}
A method is described for radioiodination to high specific activity of fixed and stained proteins within sodium dodecyl sulfate-polyacrylamide gels, without elution of the proteins from the gel. Following radioiodination, the proteins can be removed from the gel by trypsin treatment and the peptides analyzed. This procedure offers a means to structurally compare the proteins of multicomponent systems when purification of each component to homogeneity is unfeasible. Using this technique, we have… CONTINUE READING

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