A I Maneva | PubMed Health

PubMed1993

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.

Animals↗

PubMed1984

The effect of zinc on [59Fe]lactoferrin binding to blood neutrophilic leucocytes and colostral cells.

Zn2+ inhibits the binding of [59Fe]lactoferrin to neutrophilic leucocytes. The inhibiting effect is proportional to zinc concentration in the range 10-330 mumol/l. Zn2+ inhibits the [59Fe]lactoferrin binding to the colostral cells in the same degree as PMN. The inhibiting effect of Zn2+ on [59Fe]lactoferrin binding to neutrophilic leucocytes is equal to those of non-labelled lactoferrin and transferrin. Fe2+ and Cu2+ does not have such effect on binding of [59Fe]lactoferrin to the PMN leucocytes.

Cell Membrane↗

PubMed1983

Lactoferrin binding to neutrophilic polymorphonuclear leucocytes.

Neutrophilic polymorphonuclear leukocytes (PMN) bind specifically lactoferrin. This binding was characterized by two types of binding sites: with higher affinity and low capacity and another site with lower affinity and higher capacity (respectively Kaff 1 = 2.2 X 10(9) M-1 and about 39,000 binding sites per cell and Kaff2 = 0.6 X 10(9) M-1 and 76,000 binding sites per cell). The lactoferrin binding to PMN leucocytes depends on the concentration of labelled lactoferrin, the number of cells and the time for incubation. The presence of lactoferrin receptors on the PMN leucocytes is connected most probably with its effect on the cell function of these cells.

Binding Sites↗