Encyclopedia of Metalloproteins

2013 Edition
| Editors: Robert H. Kretsinger, Vladimir N. Uversky, Eugene A. Permyakov

Scandium, Interactions with Transferrin

Reference work entry
DOI: https://doi.org/10.1007/978-1-4614-1533-6_200029


This entry refers to the features of transferrin and its interactions with scandium. Transferrin is a glycoprotein found in blood plasma and milk that binds iron very tightly but reversibly to control the level of free iron in biological fluids. It has a molecular weight of around 80 kDa and contains two specific high-affinity Fe(III) binding sites. The liver is the main source of manufacturing transferrin, but other sources, e.g., the brain, also produce this molecule. The main role of transferrin is to transport iron through the blood to the liver, spleen, and bone marrow.

The transferrin was shown to bind a number of trivalent metal ions, including scandium (Perkins 1966). In vitro experiments showed that Sc3+ is bound specifically onto the iron-binding sites of transferrin, conferring on the protein similar stability to denaturants and chemical reagents as iron (Ford-Hutchinson and Perkins 1971). The binding of each Sc3+involves the ionization of two phenolic tyrosyl...

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© Springer Science+Business Media New York 2013

Authors and Affiliations

  1. 1.CAS Key Laboratory for Biomedical Effects of Nanomaterials and Nanosafety & CAS Key Laboratory of Nuclear Analytical TechniquesInstitute of High Energy Physics, Chinese Academy of SciencesBeijingChina