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Titlebook: Lactoferrin; Interactions and Bio T. William Hutchens,Bo Lönnerdal Book 1997 Humana Press Inc. 1997 Expression.Leishmania.gene expression.i

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Expression and Functional Analysis of Recombinant Human Lactoferrind processed to mature human lactoferrin by an endogenous KEX-2 peptidase. The recombinant protein retains full biological activity in terms of its ability to bind iron and human enterocyte receptors. Furthermore, the recombinant protein functions as a potent broad-spectrum antimicrobial protein.
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Difference in Binding and Fate of Lactotransferrin in Jurkat Human Lymphoblastic T-Cells and in T-47lactotransferrin; after binding at 4°C, a shift to 37°C causes cells to internalize lactotransferrin, with the maximum intracellular concentration found at 3–8 and 12–15 min for iron-saturated and iron-free forms, respectively. In contrast, epithelial breast cancer cell T-47D, which expresses low am
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The Impact of Phagocyte—Lactoferrin Interactions on Inflammationembrane containing fraction. Incubation of U937 cells with various cytokines failed to alter lactoferrin binding. We recently obtained data that human myeloid cells possess an inducible mechanism of iron acquisition from low-mol-wt chelating agents. Preliminary data suggest these cells can also acqu
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Regulation of Lymphocyte Proliferation by Lactoferrinted, but in this case, apolactoferrin had a marked restorative effect. Similar findings were observed in the CCRF-CEM T-lymphoma cell line, except that in this case, higher levels of iron were needed to inhibit proliferation. These results suggest that apolactoferrin impedes uptake of iron by the T-
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Recombinant Human Lactoferrin and Its Variants and the N-lobe with its glycosylation site (N137A) mutated. Laser-induced desorption/ionization time-of-flight mass spectrometry is used to evaluate differences between the predicted and observed molecular mass values as a function of posttranslational modification. Competitive binding experiments
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