S-Methylation of D- and L-penicillamine by human erythrocyte membrane thiol methyltransferase.

@article{Keith1985SMethylationOD,
  title={S-Methylation of D- and L-penicillamine by human erythrocyte membrane thiol methyltransferase.},
  author={Richard A. Keith and Diane M. Otterness and Adrian L Kerremans and Richard M. Weinshilboum},
  journal={Drug metabolism and disposition: the biological fate of chemicals},
  year={1985},
  volume={13 6},
  pages={669-76}
}
Human red blood cell (RBC) membranes contain a thiol methyltransferase activity that catalyzes the S-methylation of 2-mercaptoethanol (2-ME). These experiments were performed to determine whether human RBC membranes contain enzymes that can catalyze the S-methylation of D- and L-penicillamine, to determine whether those enzymes are similar to the RBC membrane thiol methyltransferase that catalyzes the S-methylation of 2-ME, and to determine whether lipophilic conjugates of the S-methyl… CONTINUE READING