A highly conserved surface loop in the C-terminal domain of ovotransferrin (residues 570-584) is remote from the receptor-binding site.

Abstract

A peptide corresponding to a surface loop in the C-terminal domain of chicken ovotransferrin (residues 570-584) was made by solid-phase synthesis and used to immunize rabbits. A 15-amino acid-residue disulphide-linked loop occurs in both domains of all five transferrins for which the sequence is available and lies on the opposite side of the iron-binding site from the interdomain cleft. Polyclonal antibodies to the peptide were specific for non-reduced holo-ovotransferrin and the C-terminal domain, as shown by e.l.i.s.a. and immunoblotting. The antibody did not inhibit binding of ovotransferrin to receptors on chick-embryo reticulocytes but was able to bind ovotransferrin bound to the cellular receptors at 0 degree C. The loop composed of residues 570-584 appears to be remote from the transferrin receptor-binding site.

Cite this paper

@article{Mason1990AHC, title={A highly conserved surface loop in the C-terminal domain of ovotransferrin (residues 570-584) is remote from the receptor-binding site.}, author={Anne B Mason and Scott Anthony Brown and William R. Church}, journal={The Biochemical journal}, year={1990}, volume={266 2}, pages={393-8} }