A highly conserved surface loop in the C-terminal domain of ovotransferrin (residues 570-584) is remote from the receptor-binding site.
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.
Mason
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AB
Department of Biochemistry, University of Vermont College of Medicine, Burlington 05405.
Brown
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SA
Church
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D000818:Animals; D001665:Binding Sites; D015153:Blotting, Western; D002642:Chick Embryo; D007158:Immunologic Techniques; D010446:Peptide Fragments / Q000276:immunology; D011990:Receptors, Transferrin / Q000378:metabolism*; D012156:Reticulocytes / Q000378:metabolism; D014168:Transferrin / Q000378:metabolism / Q000648:ultrastructure*
D010446:Peptide Fragments; D011990:Receptors, Transferrin; D014168:Transferrin