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- W2094315553 abstract "Human serum transferrin (hTF) is a single-chain bilobal glycoprotein (80 kDa) which transports Fe3+ and a variety of other metal ions in blood. Only diferric transferrin, not the apo-protein, binds strongly to transferrin receptors and is taken up by cells via receptor-mediated endocytosis. We show here that 2D [1H,13C] NMR studies of recombinant ϵ-[13C]Met-hTF allow the order of lobe loading with various metal ions, including Fe3+, to be determined. In particular, the resonance for Met-464, a residue in the hydrophobic patch of helix 5, is very sensitive to iron binding in the C-lobe. The selectivity of lobe loading with Fe3+ is compared to loading with Fe2+ (which binds as Fe3+), Al3+, Ga3+ and Bi3+. Similar changes in shifts of the Met residues are observed for these metal ions, suggesting that they induce similar conformational changes in the protein." @default.
- W2094315553 created "2016-06-24" @default.
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- W2094315553 date "1992-07-01" @default.
- W2094315553 modified "2023-10-18" @default.
- W2094315553 title "Investigations on cell metabolism of rat term decidua and metrial gland using a combination of cryo- and plastic sections" @default.
- W2094315553 doi "https://doi.org/10.1016/0143-4004(92)90183-t" @default.
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