Lactoferrin (LF) is a member of the transferrin gene family. Its expression in the mouse
uterus is regulated by estrogen and epidermal growth factor (EGF). The author et al. cloned …

Lactoferrin is present in a variety of tissues and biological fluids; however, the amount differs
significantly due to differential expressions. We have previously demonstrated that the …

Revised Manuscript Received September 27, 1993® abstract: We characterized
endocytosis of iron-saturated (holo) and iron-depleted (apo) 125I-labeled bovine lactoferrin …

Several studies suggest biological functions of the iron-binding neutrophilic glycoprotein
lactoferrin that imply an initial interaction with cells from the monocyte/macrophage family …

The BrCN cleavage of lactoferrin-a or-b (LF—a or LF—b) led to the observation of four
fragments by SDS—PAGE, whose molecular masses were 77, 58, 52, and 30 kDas, or 74 …

Transferrins (Tfs) are glycoproteins with carbohydrate chains in the C-lobe. Carbohydrate-
deficient Tfs (CDTs) with fewer sialic acids increased in several diseases. In this study, the …

Helicobacter pylori is an etiologic agent of gastritis and peptic ulcer disease in humans. We
investigated the antibacterial activities of lactoferrin and Lactoferricin®(an antimicrobial …

The interaction of apolactoferrin with hydrogen carbonate (bicarbonate) has been
investigated in the pH range 6.5–9.2. In the absence of bicarbonate apolactoferrin loses a …

We have readdressed the ability of the transferrin-binding protein B (TbpB) from Neisseria
meningitidis to discriminate between the iron-loaded and the iron-free human transferrin …

Equilibrium constants for the binding of anions to apotransferrin, to the recombinant N-lobe
half transferrin molecule (Tf/2N), and to a series of mutants of Tf/2N have been determined …