[Comparative characteristics of molecular forms of human thyroxine-binding globulin].
Two molecular variants, of thyroxin-binding globulin (TBG), TBG-1 and TBG-2, were obtained from human retroplacental blood by fractionation of pure TBG on concanavalin A-Sepharose. It was found that both variants are immunologically identical, have similar molecular weights, amino acid composition and spectral properties, and possess the same affinity for thyroid hormones. However, TBG-1 and TBG-2 differed in charge upon isoelectrofocusing and had different monosaccharide composition. The existence of two molecular variants of TBG in pregnancy is probably due to the peculiarities of the polypeptide chain glycosylation during TBG biosynthesis.
D000595:Amino Acid Sequence; D002846:Chromatography, Affinity; D002942:Circular Dichroism; D004591:Electrophoresis, Polyacrylamide Gel; D005260:Female; D006801:Humans; D007525:Isoelectric Focusing; D008970:Molecular Weight; D009005:Monosaccharides / Q000032:analysis; D011233:Precipitin Tests; D011247:Pregnancy; D011257:Pregnancy Proteins / Q000032:analysis; D013056:Spectrophotometry, Ultraviolet; D013975:Thyroxine-Binding Proteins / Q000032:analysis*
D009005:Monosaccharides; D011257:Pregnancy Proteins; D013975:Thyroxine-Binding Proteins
Sravnitel'naia kharakteristika molekuliarnykh raznovidnosteĭ tiroksinsviazyvaiushchego globulina cheloveka.