Elementary chain composition of guinea pig thyroglobulin.
Thyroglobulin obtained from guinea pigs was examined by Na dodecyl-SO4-polyacrylamide gel electrophoresis after reduction and alkylation. In contrast to thyroglobulin from other mammalian sources, only three groups of polypeptide chains accounted for 95% or more of the protein. Determinations of the molecular weights of these purified proteins by equilibrium centrifugation in 6 M guanidine HCl gave values of 295,000 (species A), 210,000 (species B), and 110,000 (species C). Molecular weights determined by gel filtration in 6 M guanidine HCl gave similar results. Due to the large size of the polypeptides, satisfactory molecular weights could not be obtained from Na dodecyl-SO4-polyacrylamide gel electrophoresis. Amino acid analysis of the three species was similar to that of whole thyroglobulin. Only slightly higher level of lysine and histidine and a lower level of glutamic acid were seen in species C. The iodine contents were found to range from 0.07 to 0.12 to 0.20% for species A, B, and C, respectively.
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D004591:Electrophoresis, Polyacrylamide Gel; D006168:Guinea Pigs; D007455:Iodine / Q000032:analysis; D046911:Macromolecular Substances; D008970:Molecular Weight; D013954:Thyroglobulin / Q000032:analysis
D000596:Amino Acids; D046911:Macromolecular Substances; D013954:Thyroglobulin; D007455:Iodine