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- W2028431204 abstract "27Al NMR spectroscopy has been used to study the binding of aluminum to the human serum proteins albumin and transferrin. A signal was observed for Al3+ bound to albumin and from the maximum intensity of this signal it is concluded that $̃3 Al3+ ions are bound to each albumin. Comparison of the chemical shift of the Al3+-albumin signal with those for small Al3+ containing complexes indicates that the albumin Al3+ is octahedrally coordinated by oxygen atoms. No recognizable signal was observed for Al3+ bound to transferrin. It is suggested that this is because the bound Al3+ exists in a site of low symmetry and consequently its NMR signal is considerably broadened by quadrupole induced relaxation." @default.
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- W2028431204 date "1992-04-01" @default.
- W2028431204 modified "2023-09-23" @default.
- W2028431204 title "A 27Al NMR investigation of Al3+ binding to small carboxylic acids and the proteins albumin and transferrin" @default.
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- W2028431204 doi "https://doi.org/10.1016/0162-0134(92)80061-y" @default.
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