Isolation and sequences of the cysteinyl tryptic peptides from the MoFe-protein of Azotobacter vinelandii nitrogenase.

@article{Lundell1981IsolationAS,
  title={Isolation and sequences of the cysteinyl tryptic peptides from the MoFe-protein of Azotobacter vinelandii nitrogenase.},
  author={Daniel J. Lundell and James W. Howard},
  journal={The Journal of biological chemistry},
  year={1981},
  volume={256 12},
  pages={6385-91}
}
The cysteinyl residues in the alpha and beta subunits of the MoFe-protein from Azotobacter vinelandii nitrogenase were radiolabeled by carboxymethylation with iodo[14C]acetic acid. The tryptic peptides from the isolated subunits were separated by ion-exchange chromatography on DEAE-Sephadex and SP-Sephadex. The radiolabeled (cysteinyl) peptides were sequenced by Edman degradation. The isolation procedure and sequences of the peptides provide a method for the identification of the potential… CONTINUE READING