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 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.
Kiss
Tamás
T
Department of Inorganic and Analytical Chemistry, University of Szeged, Szeged, Hungary.
Jakusch
Tamás
T
Hollender
Dominik
D
Enyedy
Eva Anna
EA
Horváth
László
L
D018360:Crystallography, X-Ray; D006801:Humans; D006863:Hydrogen-Ion Concentration; D007004:Hypoglycemic Agents / Q000737:chemistry*; D012709:Serum Albumin / Q000378:metabolism; D014168:Transferrin / Q000378:metabolism; D017968:Vanadium Compounds / Q000737:chemistry*; D017967:Zinc Compounds / Q000737:chemistry*
D007004:Hypoglycemic Agents; D012709:Serum Albumin; D014168:Transferrin; D017968:Vanadium Compounds; D017967:Zinc Compounds