title: Binding affinity of monoiodinated insulin tracers isolated after reversed-phase high-performance liquid chromatography.
abstract: Insulin and insulin monoiodinated in tyrosine A14, A19, B16 and B26 can be separated using reversed-phase high-performance liquid chromatography on a number of C18 columns eluted with acetonitrile containing triethylammonium phosphate or acetate buffers. The monoiodoinsulins can be isolated using lyophilization, gel chromatography, or Sep-Pak purification. Compared with similar tracers purified and isolated by disc electrophoresis-ion-exchange chromatography, the resulting binding affinities to adipocytes of the purified tracers are more or less reduced dependent on the choice of column support, buffer, separation temperature, and isolation procedure.
mesh_terms: D000818:Animals; D002846:Chromatography, Affinity / Q000379:methods; D002851:Chromatography, High Pressure Liquid / Q000379:methods; D002852:Chromatography, Ion Exchange / Q000379:methods; D004589:Electrophoresis, Disc; D007328:Insulin / Q000031:analogs & derivatives* / Q000302:isolation & purification; D011485:Protein Binding; D013552:Swine; D013696:Temperature
chemical_list: D007328:Insulin; C008147:insulin, iodo-