Summary
When lactoferrin (Lf) is tagged with a residualizing label and injected intravenously in rats, the label is recovered almost exclusively with the liver. The plasma clearance curve of Lf comprises two components: a rapid initial one, followed by a slower one. Analyses of plasma samples by gel filtration suggest the slower component to be the result of complex formation between Lf and plasma proteins. The possibility is raised that these complexes are not targeted to the same cells as uncomplexed Lf. Since hepatic heparan sulfate proteoglycan binds strongly to Lf, it seems likely that this plasmalemma constituent serves as a nonspecific binding site for Lf. Only minute amounts of Lf are absorbed from the peritoneal cavity. Overall, the metabolic observations indicate that despite a close structural relatedness between Lf and transferrin (Tf), the functions of both proteins differ greatly.
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Regoeczi, E. (1997). Observations on the Metabolism and Cellular Interactions of Lactoferrin. In: Hutchens, T.W., Lönnerdal, B. (eds) Lactoferrin. Experimental Biology and Medicine, vol 28. Humana Press. https://doi.org/10.1007/978-1-4612-3956-7_22
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DOI: https://doi.org/10.1007/978-1-4612-3956-7_22
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