The origin of the electrophoretic doublet of thyroglobulin.
Bovine and human thyroglobulin show two closely migrating bands in reducing SDS-PAGE. Limited digestion with chymotrypsin, trypsin and thermolysin converted the slower band of the doublet into a peptide identical to the faster band, with an apparent mass of 270 kDa, in both species. The starting point of the faster band of the doublet was established at Ileu 520 with native bovine Tg and at Ser 503 with native human Tg, and at Ser 503 and Ser 504 with chymotrypsin-digested bovine and human Tg, respectively. These data explain the electrophoretic heterogeneity of thyroglobulin and unveil a region highly susceptible to proteolysis at about 500 residues from the NH2-terminus of the molecule.
Gentile
F
F
Centro di Endocrinologia e Oncologia Sperimentale del C.N.R., University of Naples 2nd Medical School, Italy.
Palumbo
G
G
Salvatore
G
G
D000595:Amino Acid Sequence; D000818:Animals; D002417:Cattle; D004591:Electrophoresis, Polyacrylamide Gel / Q000379:methods; D010450:Endopeptidases; D006801:Humans; D046911:Macromolecular Substances; D008969:Molecular Sequence Data; D008970:Molecular Weight; D010446:Peptide Fragments / Q000302:isolation & purification; D012689:Sequence Homology, Nucleic Acid; D013954:Thyroglobulin / Q000737:chemistry* / Q000302:isolation & purification
D046911:Macromolecular Substances; D010446:Peptide Fragments; D013954:Thyroglobulin; D010450:Endopeptidases