Domain-specific monoclonal antibodies to ovotransferrin indicate conservation of determinants involved in avian transferrin receptor recognition.
1. Three of five monoclonal antibodies produced to chicken ovotransferrin bound quail ovotransferrin but none of the antibodies bound human, bovine or equine serum transferrin. 2. Equilibrium binding experiments indicate that both quail and chicken ovotransferrin bind to transferrin receptors on chick reticulocytes although the quail protein binds to 40% fewer sites with an affinity which is three times lower than chicken ovotransferrin. 3. The antibodies that recognize quail ovotransferrin block binding of both radiolabelled chicken and quail ovotransferrin to chick reticulocytes. 4. Quail NH2-terminal half-molecule domain appears to be unable to form a functional hybrid holo-ovotransferrin with chicken C-terminal half-molecule domain.
Mason
A B
AB
Department of Biochemistry, University of Vermont College of Medicine, Burlington 05405.
Brown
S A
SA
Church
W R
WR
D000818:Animals; D000911:Antibodies, Monoclonal; D000918:Antibody Specificity; D001667:Binding, Competitive; D005075:Biological Evolution; D002645:Chickens; D003207:Conalbumin / Q000235:genetics / Q000276:immunology / Q000378:metabolism*; D003429:Cross Reactions; D004527:Egg Proteins / Q000378:metabolism*; D000939:Epitopes / Q000235:genetics; D004912:Erythrocytes / Q000378:metabolism; D011784:Quail; D011990:Receptors, Transferrin / Q000378:metabolism*; D013045:Species Specificity
D000911:Antibodies, Monoclonal; D004527:Egg Proteins; D000939:Epitopes; D011990:Receptors, Transferrin; D003207:Conalbumin