Comparison of human lactoferrins from milk and neutrophilic leucocytes. Relative molecular mass, isoelectric point, iron-binding properties and uptake by the liver.
Human lactoferrins isolated from neutrophilic leucocytes and milk by CM-Sephadex chromatography were similar in Mr (76000) and pI (8.7). Upon acidification, both proteins released their two Fe3+ ions/molecule in a similar biphasic way. Both proteins intravenously injected into mice were cleared from plasma at the same rate. The maximal uptakes by the liver, which occurred 5 min after injection, were inhibited to the same extent by milk lactoferrin used as a competitor.
D000818:Animals; D004591:Electrophoresis, Polyacrylamide Gel; D006801:Humans; D007501:Iron / Q000378:metabolism; D007526:Isoelectric Point; D007781:Lactoferrin / Q000302:isolation & purification / Q000378:metabolism*; D007782:Lactoglobulins / Q000378:metabolism*; D008099:Liver / Q000378:metabolism; D046911:Macromolecular Substances; D051379:Mice; D008807:Mice, Inbred BALB C; D008892:Milk / Q000032:analysis*; D008970:Molecular Weight; D009504:Neutrophils / Q000032:analysis*
D007782:Lactoglobulins; D046911:Macromolecular Substances; D007501:Iron; D007781:Lactoferrin