The isoelectric focusing of human thyroglobulin.
The isoelectric focusing of human thyroglobulin has been studied on slab gels. Three bands, focusing between pH 4.4 and 4.7, are observed. Deglycosylation of thyroglobulin does not affect the distribution of focused bands, but increases the pH range of focusing slightly. Native thyroglobulin and its half-sized subunit show the same distribution of isoelectric bands. Refocusing of one band results in the appearance of the three original bands. It appears that soluble complexes of thyroglobulin with ampholyte account for the apparent heterogeneity observed on isoelectric focusing.
D000665:Ampholyte Mixtures; D006026:Glycoside Hydrolases; D006801:Humans; D006863:Hydrogen-Ion Concentration; D007525:Isoelectric Focusing; D011489:Protein Denaturation; D013954:Thyroglobulin / Q000302:isolation & purification*
D000665:Ampholyte Mixtures; D013954:Thyroglobulin; D006026:Glycoside Hydrolases