Comparative studies on the biospeciation of antidiabetic VO(IV) and Zn(II) complexes

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...

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Bibliographic Details
Published in:Journal of inorganic biochemistry 2009-04, Vol.103 (4), p.527-535
Main Authors: Kiss, Tamás, Jakusch, Tamás, Hollender, Dominik, Enyedy, Éva Anna, Horváth, László
Format: Article
Language:English
Subjects:
Biospeciation
Crystallography, X-Ray
Humans
Hydrogen-Ion Concentration
Hypoglycemic Agents - chemistry
Insulin-mimesis
Serum Albumin - metabolism
Transferrin - metabolism
Ultrafiltration
Vanadium Compounds - chemistry
VO(IV) complexes
Zinc Compounds - chemistry
Zn(II) complexes
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Summary: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.
ISSN:0162-0134
1873-3344
DOI:10.1016/j.jinorgbio.2008.11.006