Tryptophan Synthetase , & Subunit PRIMARY STRUCTURE OF THE PYRIDOXYL PEPTIDE FROM THE ESCHERICHIA COLI ENZYME *

@inproceedings{Fluri2003TryptophanS,
  title={Tryptophan Synthetase , & Subunit PRIMARY STRUCTURE OF THE PYRIDOXYL PEPTIDE FROM THE ESCHERICHIA COLI ENZYME *},
  author={Rudolf Fluri and Laura E Jackson and Whitney E Lee and I. P. Crawford},
  year={2003}
}
Radioactivity incorporated into an e-N-5’-phosphopyridoxyllysine residue of the /3 chain by reduction of the flZ holoenzyme with tritiated sodium borohydride appears in two tryptic peptides. These pyridoxyl peptides differ by only a single arginyl residue. As expected, tryptic digests of normal protein contain two peptides that together make up the… CONTINUE READING