Selective phenylglyoxalation of functionally essential arginyl residues in the erythrocyte anion transport protein

@article{Bjerrum1983SelectivePO,
  title={Selective phenylglyoxalation of functionally essential arginyl residues in the erythrocyte anion transport protein},
  author={P. J. Bjerrum and J. O. Wieth and Charles L Borders},
  journal={The Journal of General Physiology},
  year={1983},
  volume={81},
  pages={453 - 484}
}
The red cell anion transport protein, band 3, can be selectively modified with phenylglyoxal, which modifies arginyl residues (arg) in proteins, usually with a phenylglyoxal: arg stoichiometry of 2:1. Indiscriminate modification of all arg in red cell membrane proteins occurred rapidly when both extra- and intracellular pH were above 10. Selective modification of extracellularly exposed arg was achieved when ghosts with a neutral or acid intracellular pH were treated with phenylglyoxal in an… CONTINUE READING

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