Polypeptide chain composition of thyroglobulin

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Abstract
Thyroglobulin can be dissociated into a component which appears to be a half molecule (12 S) of the undissociated molecule (19 S). These 2 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 2 closely migrating bands, both having an apparent MW 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 were obtained with both hog and rat thyroglobulin.