Effect of bovine milk antigens and egg lysozyme on the binding of 59Fe-lactoferrin to platelet plasma membranes.

1. Platelets bind specifically to lactoferrin. A significant similarity between human lactoferrin and some bovine milk proteins has been established. 2. Because of the structural homology of lactoferrin and cows milk proteins they are able to influence lactoferrins regulatory function on the level of its binding to membrane receptors on platelets. 3. An inhibitory effect of bovine alpha-lactalbumin and of beta-lactoglobulin on lactoferrin-receptor interaction was shown. 4. Bovine alpha-lactalbumin competes with lactoferrin for the binding sites. 5. Scatchard plot analysis of data shows one binding site for lactoferrin in the presence of alpha-lactalbumin with an affinity constant, Ka = 0.46 x 10(9) mol/l and 335 receptors/cell. 6. The inhibitory effect of beta-lactoglobulin reaches 62% and is different for the common fraction beta-lactoglobulin and the genetic variants beta-lactoglobulin A and B. 7. beta-lactoglobulin does not compete with lactoferrin for the membrane receptors. 8. Bovine casein and egg lysozyme stimulate 59Fe-lactoferrin binding to the receptors. The mechanism of these effects is still unknown. 9. Tested alimentary antigens are able to interact with lactoferrin and also with some platelet membrane structures. 10. Established changes in lactoferrin binding to the platelet membrane might be in relation to lactoferrins regulatory function and (or) eliminating mechanisms of these alimentary antigens.