Protein modification by diazotized arsanilic acid: synthesis and characterization of the phenylthiohydantoin derivatives of azobenzene arsonate-coupled tyrosine, histidine, and lysine residues and their sequential allotment in labeled peptides.

@article{Schwaller1989ProteinMB,
  title={Protein modification by diazotized arsanilic acid: synthesis and characterization of the phenylthiohydantoin derivatives of azobenzene arsonate-coupled tyrosine, histidine, and lysine residues and their sequential allotment in labeled peptides.},
  author={Beat Schwaller and Hans Sigrist},
  journal={Analytical biochemistry},
  year={1989},
  volume={177 1},
  pages={
          183-7
        }
}
1 Citations

References

SHOWING 1-10 OF 16 REFERENCES

Topography of the external surface of the human red blood cell membrane studied with a nonpenetrating label, [125I]diazodiiodosulfanilic acid.

Its reactions provide further evidence of the organizational complexity of the red cell membrane and emphasize the fact that interpretation of information derived from the use of membrane probes must take into account the differences resulting from the properties of the probing reagents themselves.

Effects of pH and temperature on the interaction of an impermeant probe with surface proteins of the human red blood cell.

The data presented emphasize the lability of membrane conformation and reactivity and thus the necessity to consider carefully the conditions of labeling in interpretation of studies using impermeant probes.