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- W2321734580 abstract "in the serum before addition of the iron or indium, however, after addition of the metal ions the transferrins migrated as a single fast-moving species. Urea/gel electrophoresis has also been used to investigate the ability of In( I l l ) to displace Zn(l l ) from ovotransferrin. Although zinc binds specifically to the protein, the zinc complex was unstable on the polyacrylamide gel and migrated as the metal-free protein. When a two-fold excess of indium chloride was added to zinc-saturated ovotransferrin the zinc was displaced completely as judged by the mobility of the protein upon urea/gcl clectrophoresk. T h e results of this study show that In(llI) forms tight complexes with both human serum transferrin and hen ovotransferrin which retain the indium upon electrophoresis in the presence o f 6 M-urea. This technique can therefore be used to investigate the ability of transferrin to remove indium from chelators whch are currently being developed for use as indium-labelled pharmaceuticals." @default.
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- W2321734580 date "1988-10-01" @default.
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- W2321734580 title "Characterization of the amino acid change in a transferrin variant" @default.
- W2321734580 doi "https://doi.org/10.1042/bst0160834" @default.
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