Polypeptide chain composition of thyroglobulin.
It is known that thyroglobulin can be dissociated into a component which appears to be a half molecule (12 S) of the undissociated molecule (19 S). In the present work, these two molecular species were isolated with a high degree of purity by preparative gel electrophoresis in sodium dodecyl sulfate and were individually reduced. The reduction pattern of the 12 S form displayed only two closely migrating bands, both having an apparent Mr near 330 000, whereas the undissociated (covalently linked) 19 S form showed a complex pattern consisting of, besides the 330 000 doublet, nonreducible material and several faster bands, resembling the pattern of the unfractionated protein. The origin of the faster-moving peptides is not known. These results have been obtained with both hog and rat thyroglobulin.
D000818:Animals; D004591:Electrophoresis, Polyacrylamide Gel; D008623:Mercaptoethanol; D010455:Peptides / Q000032:analysis / Q000302:isolation & purification; D011489:Protein Denaturation; D051381:Rats; D013552:Swine; D013954:Thyroglobulin / Q000032:analysis*
D010455:Peptides; D008623:Mercaptoethanol; D013954:Thyroglobulin