抄録
The possibility of using recombinant human lactoferrin from rice (rhLF) makes it necessary to study its differences from the protein of milk. In this work, the binding of different iron-saturated forms of rhLF to Caco-2 cells was studied. Iron-saturated rhLF bound in higher proportion than the apo-form, but, the data obtained for specific binding were not compatible with receptor-mediated binding. Competition assays showed the same binding capacity for human milk lactoferrin as for rhLF to Caco-2 cells. Another basic protein of milk, lactoperoxidase, was found to compete with rhLF for binding to Caco-2 cell membranes, suggesting an electrostatic interaction. The transport of iron (59Fe) bound to rhLF and to citrate and the transport of rhLF (125I-labeled) were studied on Caco-2 monolayers. Transport of iron was found to be significantly greater when bound to citrate than to rhLF. The amount of intact lactoferrin that traversed the Caco-2 monolayers was very low, suggesting degradation of it across these cells.
