[New aspects of isolation and purification of thyroxine-binding globulin from human biological fluids].
Based on the new data concerning the multicomponent system of thyroxine-binding proteins in human plasma, some methodological aspects of isolation and purification of thyroxine-binding globulin (TBG) were examined, and a simple two-step procedure for TBG purification was developed. Normal human blood serum, retroplacental serum and amniotic fluid were used as TBG sources. The procedure includes affinity chromatography and adsorption chromatography on a hydroxyapatite column. A biospecific adsorbent was synthesized by stepwise binding of epichlorohydrin and thyroxine to Sepharose. The yield of pure TBG varied from 60 to 80%, depending on the TBG source used. The properties of TBG preparations from retroplacental serum and amniotic fluid were identical; both preparations contained a pregnancy-associated molecular variant, TBG-1. Two novel serum thyroxine-binding proteins were detected, isolated and partly characterized.
Sviridov
O V
OV
Ermolenko
M N
MN
Strel'chenok
O A
OA
D000596:Amino Acids / Q000032:analysis; D000653:Amniotic Fluid / Q000032:analysis*; D001826:Body Fluids / Q000032:analysis*; D002846:Chromatography, Affinity; D002850:Chromatography, Gel; D005260:Female; D006801:Humans; D011247:Pregnancy; D013975:Thyroxine-Binding Proteins / Q000302:isolation & purification*
D000596:Amino Acids; D013975:Thyroxine-Binding Proteins
Novye aspekty vydeleniia i ochistki tiroksinsviazyvaiushchego globulina iz biologicheskikh zhidkosteĭ cheloveka.