Comparative binding study of aluminum and chromium to human transferrin. Effect of iron.
Article Details
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Moshtaghie AA, Ani M, Bazrafshan MR
Comparative binding study of aluminum and chromium to human transferrin. Effect of iron.
Biol Trace Elem Res. 1992 Jan-Mar;32:39-46.
- PubMed ID
- 1375080 [ View in PubMed]
- Abstract
The characteristics of aluminum and chromium binding to apo-transferrin (apo-tf) have been investigated and compared. Both metal ions were taken up by human transferrin forming complexes with the maximum absorbances at 405 nm for chromium-transferrin (cr-tf) and 240 nm for aluminum-transferrin (Al-tf). In the presence of citric acid, chromium binding to transferrin is five times more than aluminum. The binding of aluminum or chromium to apo-transferrin was reduced by 18 and 22% in the presence of 200 ng/mL of iron. The binding of both metals to apo-tf appears to be pH dependent. In acidic pHs, less chromium and more aluminum binding occurred.
DrugBank Data that Cites this Article
- Drug Carriers
Drug Carrier Kind Organism Pharmacological Action Actions Chromic citrate Serotransferrin Protein Humans UnknownNot Available Details Chromic nitrate Serotransferrin Protein Humans UnknownNot Available Details Chromium Serotransferrin Protein Humans UnknownBinderDetails Chromium gluconate Serotransferrin Protein Humans UnknownNot Available Details Chromium nicotinate Serotransferrin Protein Humans UnknownNot Available Details Chromous sulfate Serotransferrin Protein Humans UnknownNot Available Details