The binding of 99mTc(Sn)-MDP complexes to human serum albumin and other blood proteins determined with gel chromatography and ultrafiltration.
The binding of 99mTc(Sn)-MDP to human serum albumin and other blood proteins was investigated by gel chromatography and ultrafiltration. During gel chromatography dissociation of the 99mTc(Sn)-MDP-protein complex occurs: thus, it is not a suitable technique for the determination of protein binding. The values found with ultrafiltration have to be corrected for non-ultrafiltrable TcO2.nH2O. From the corrected values it can be concluded that binding of 99mTc(Sn)-MDP to blood proteins does not play a role in the biodistribution.
Huigen
Y M
YM
Analytical Chemistry Laboratory, State University of Utrecht, The Netherlands.
Tji
T G
TG
Gelsema
W J
WJ
de Ligny
C L
CL
D001798:Blood Proteins / Q000378:metabolism*; D002850:Chromatography, Gel; D006801:Humans; D012709:Serum Albumin / Q000378:metabolism*; D013669:Technetium Tc 99m Medronate / Q000378:metabolism*; D014462:Ultrafiltration
D001798:Blood Proteins; D012709:Serum Albumin; C023568:technetium Tc 99m (Sn)methylenediphosphonate; D013669:Technetium Tc 99m Medronate