Study of the binding of 114mIn radiotracer to human serum components by ultrafiltration and chromatography.
The chemical speciation of indium in serum was studied. Ultrafiltration was used to investigate the influence of several buffer systems on the binding characteristics of indium in serum and to study the association of indium with transferrin and albumin. This was performed by means of batch incubation experiments with a 114mIn tracer. Different buffer systems were investigated. A series of bicarbonate, Tris:HCl and HEPES buffers were found to fit for this purpose. Phosphate buffer was not suitable, as it is capable of disrupting the binding between indium and transferrin. Batch ultrafiltration experiments with 114mIn incubated solutions of transferrin and albumin showed that both proteins are capable of binding indium to a high degree. Three chromatographic techniques (SEC, AEC, AC) were used to study the different chemically active species of indium in serum. It is concluded that next to transferrin, albumin is also responsible for the binding and transport of indium in serum.
Van Hulle
M
M
Laboratory for Analytical Chemistry, Ghent University, Belgium. marijn.vanhulle@rug.ac.be
De Cremer
K
K
Cornelis
R
R
D002846:Chromatography, Affinity / Q000379:methods*; D002850:Chromatography, Gel / Q000379:methods*; D006801:Humans; D007205:Indium Radioisotopes / Q000378:metabolism*; D011485:Protein Binding; D012709:Serum Albumin / Q000378:metabolism*; D014168:Transferrin / Q000378:metabolism*; D014462:Ultrafiltration
D007205:Indium Radioisotopes; D012709:Serum Albumin; D014168:Transferrin