2010
DOI: 10.1016/j.jlumin.2010.07.015
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Spectroscopic analysis of the interaction between chromium (III) and apoovotransferrin

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Cited by 11 publications
(1 citation statement)
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“…54,182,193 Another limitation of all these analytical techniques is their poor sensitivities (require mM concentrations of V), 182 although computer modelling can be used to extrapolate the results to biologically relevant V concentrations (low mM range). 194,195 Early electronic and EPR spectroscopic data, 196 supported by more recent data, 197 showed that Cr(III) is capable of binding specifically to Fe(III) binding sites of transferrin. Hence, this was assumed to act as the main Cr(III) transport protein, at a time it was considered as essential.…”
Section: Mammalian Metabolism and Speciation Of Anti-diabetic Metal C...mentioning
confidence: 77%
“…54,182,193 Another limitation of all these analytical techniques is their poor sensitivities (require mM concentrations of V), 182 although computer modelling can be used to extrapolate the results to biologically relevant V concentrations (low mM range). 194,195 Early electronic and EPR spectroscopic data, 196 supported by more recent data, 197 showed that Cr(III) is capable of binding specifically to Fe(III) binding sites of transferrin. Hence, this was assumed to act as the main Cr(III) transport protein, at a time it was considered as essential.…”
Section: Mammalian Metabolism and Speciation Of Anti-diabetic Metal C...mentioning
confidence: 77%