Molecular interactions between human lactotransferrin and the phytohemagglutinin-activated human lymphocyte lactotransferrin receptor lie in two loop-containing regions of the N-terminal domain I of human lactotransferrin.

@article{Legrand1992MolecularIB,
  title={Molecular interactions between human lactotransferrin and the phytohemagglutinin-activated human lymphocyte lactotransferrin receptor lie in two loop-containing regions of the N-terminal domain I of human lactotransferrin.},
  author={Dominique Legrand and Jo{\"e}l Mazurier and Abdelaziz Elass and Eric B. Rochard and G{\'e}rard Vergoten and Patricia Maes and Jean Montreuil and Genevi{\'e}ve Spik},
  journal={Biochemistry},
  year={1992},
  volume={31 38},
  pages={
          9243-51
        }
}
  • Dominique Legrand, Joël Mazurier, +5 authors Geneviéve Spik
  • Published in Biochemistry 1992
  • Chemistry, Medicine
  • Fluorescein isothiocyanate derivatization of the human lactotransferrin on Lys-264 inhibits the binding of the protein of human PHA-activated lymphocytes [Legrand, D., Mazurier, J., Maes, P., Rochard, E., Montreuil, J., & Spik, G. (1991) Biochem. J. 276, 733-738], indicating that part of the receptor-binding site is located in the N-terminal domain I of lactotransferrin. In the present study, a 6-kDa peptide (residues 4-52) was isolated from the N-terminal lobe of human lactotransferrin which… CONTINUE READING

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