Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
1317421 | Journal of Inorganic Biochemistry | 2009 | 9 Pages |
Abstract
The speciation of several insulin-mimetic/enhancing VO(IV) and Zn(II) complexes in human blood serum was studied and a comparison was made concerning the ability of the serum components to interact with the original metal complexes and the distribution of the metal ions between the low and the high molecular fractions of the serum. It was found that the low molecular mass components may play a larger role in transporting Zn(II) than in the case with VO(IV). Among the high molecular mass serum proteins, transferrin is the primary binder of VO(IV), and albumin is that of Zn(II). The results revealed that protein–ligand interactions may influence the metal ion distribution in the serum.
Related Topics
Physical Sciences and Engineering
Chemistry
Inorganic Chemistry
Authors
Tamás Kiss, Tamás Jakusch, Dominik Hollender, Éva Anna Enyedy, László Horváth,