Summary
Lactoferrin (Lf) is a major milk whey protein in humans, but in some species (rabbit and rat) is virtually undetectable, whereas transferrin (Tf) is present at a high concentration in rabbit and mouse milk, but is undetectable in human milk. In order to determine whether the Lf gene is expressed in rat tissues, a lactating rat mammary gland cDNA library in λgt10 was screened both with partial cDNAs of rat liver Tf and human Lf, respectively. No positive clones were found with the latter probe, indicating that Lf is not expressed by rat mammary gland or at an undetectable level. The screening with the Tf probe led to the obtention of a 2275-bp insert coding for an open reading frame of 695 amino acid residues. This includes a 19 amino acid signal sequence, and the mature protein contains 676 amino acids and one N-glycosylation site in the C-terminal domain at residue 490.
The native rat milk Tfs are separated into four bands on native PAGE that differ only in their sialic acid content. The structures of the glycans from two major variants were completely determined by 400 MHz 1H-NMR spectroscopy. They contain, respectively, one and two neuraminic acid residues (α 2–6) linked to galactose in conventional biantennary N-acetyllactosamine-type glycans. Both contain a fucose (α 1–6) linked to the terminal nonreducing N-acetylglucosamine.
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Pierce, A. et al. (1997). Lactoferrin Almost Absent from Lactating Rat Mammary Gland is Replaced by Transferrin. 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_9
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