Role of sialic acid in the microheterogeneity of serum thyroxine-binding globulin. Study by two-dimensional isoelectric focusing.
A new technique combining a neuraminidase treatment of thyroxine-binding globulin after serum isoelectric focusing and a second-dimensional isoelectric focusing was developed to study the role of sialic acid in the microheterogeneity of native thyroxine-binding globulin. By showing the change of PI occasioned by the desialylation for each of the bands constituting the thyroxine-binding globulin pattern separately, this procedure clearly demonstrated that the microheterogeneity of the native protein could not be imputed to the varying sialic acid content of the bands only. We suggest that at least three molecules of thyroxine-binding globulin, with probably slight differences in their amino acid composition, are present in the serum, and that different degrees of sialylation ensure greater microheterogeneity of this protein.
D000328:Adult; D000510:Alpha-Globulins / Q000032:analysis*; D005260:Female; D006801:Humans; D007525:Isoelectric Focusing; D007526:Isoelectric Point; D009439:Neuraminidase / Q000378:metabolism; D012794:Sialic Acids / Q000378:metabolism*; D013975:Thyroxine-Binding Proteins / Q000032:analysis*
D000510:Alpha-Globulins; D012794:Sialic Acids; D013975:Thyroxine-Binding Proteins; D009439:Neuraminidase