Guinea pig thyroglobulin: Molecular weight of subunits and amino acid and sugar compositions
1977; Elsevier BV; Volume: 77; Issue: 3 Linguagem: Inglês
10.1016/s0006-291x(77)80059-4
ISSN1090-2104
Autores Tópico(s)Protein Hydrolysis and Bioactive Peptides
ResumoA reevaluation of the molecular weights of the three major subunits of guinea pig thyroglobulin has been undertaken in gels of varying concentration. Since the apparent molecular weights determined from plots of relative mobility versus log molecular weight were found to decrease as the gel porosity decreased, the relationship of retardation coefficient to molecular weight was used. Molecular weights obtained by this technique were 192,000, 131,000, and 121,000; these were close to the values obtained from electrophoresis in 8% gels. Amino acid and sugar compositions are also reported; the guinea pig protein, like that from human thyroids, contains galactosamine in addition to glucosamine, suggesting that it contains three types of saccharide units. Aminoterminal analyses performed by dinitrophenylation indicated nonstoichiometric amounts of aspartic acid, leucine and serine.
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