Methyl acceptors for protein methylase II from human-erythrocyte membrane.

@article{Galletti1979MethylAF,
  title={Methyl acceptors for protein methylase II from human-erythrocyte membrane.},
  author={Patrizia Galletti and W Ki Paik and Sangduk Kim},
  journal={European journal of biochemistry},
  year={1979},
  volume={97 1},
  pages={221-7}
}
Membrane proteins from human erythrocytes were methylated with purified protein methylase II (S-adenosylmethionine:protein-carboxyl O-methyltransferase, EC.2.1.1.24). The methylated proteins were analyzed by dodecyl sulfate/polyacrylamide gel electrophoresis. Monomeric and dimeric glycophorin A (NaIO4/Schiff-2 and NaIO4/Schiff-1 positive bands) and 'band 4.5' were identified as two major classes of methyl-acceptor polypeptides for protein methylase II. In rabbit erythrocyte membrane where… CONTINUE READING

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