Iron binding to human lactoferrin alters reactivity of the protein with plant lectins.
Binding of Fe by human apolactoferrin results in altered reactivity of the glycoprotein with plant lectins. Reaction with wheat germ agglutinin (WGA) and peanut agglutinin (PNA) was abolished with Fe binding. Reaction with the lectins from Datura stramonium (DSA) and Aleuria aurantia (AAA) was significantly reduced but not fully abolished on Fe binding, while reaction with the Artocarpus integrifolia lectin (Jacalin) and Sambucus nigrabark (SNA) was not changed at all. Loss of WGA reactivity occurred when only one of two Fe binding sites on the molecule was saturated. The results demonstrate conformational changes that are associated with high-avidity binding of Fe by lactoferrin.
Ying
L
L
Department of Biology, New York University, New York 10003.
Furmanski
P
P
D000911:Antibodies, Monoclonal; D001059:Apoproteins / Q000302:isolation & purification / Q000378:metabolism*; D015153:Blotting, Western; D004591:Electrophoresis, Polyacrylamide Gel; D004797:Enzyme-Linked Immunosorbent Assay; D006801:Humans; D007501:Iron / Q000378:metabolism*; D007700:Kinetics; D007781:Lactoferrin / Q000302:isolation & purification / Q000378:metabolism*; D037102:Lectins / Q000302:isolation & purification; D011485:Protein Binding; D012710:Serum Albumin, Bovine / Q000378:metabolism; D013329:Structure-Activity Relationship
D000911:Antibodies, Monoclonal; D001059:Apoproteins; D037102:Lectins; C039223:apolactoferrin; D012710:Serum Albumin, Bovine; D007501:Iron; D007781:Lactoferrin