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April 1, 2026

Chemical and Physical Characterization of Submolecular Proteins of Porcine Thyroglobulin

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Authors

EIEiji ItagakiMAMasatoshi ArisawaKao Corporation (Japan)THToichiro Hosoya

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Overview

Analysis reveals distinct submolecular proteins in thyroglobulin, suggesting similarities in structure and function.

Key Points

  • This research aims to characterize the submolecular proteins of porcine thyroglobulin chemically and physically.
  • Conducted polyacrylamide gel electrophoresis in SDS to identify protein bands.
  • Dialyzed thyroglobulin against distilled water to analyze changes in molecular weight.
  • Isolated submolecular components using gel filtration on Sephadex G-200.
  • Confirmed homogeneity of proteins by sedimentation equilibrium analysis.
  • Identified over ten distinct bands of thyroglobulin in the weight range of 19,000 to 330,000.
  • Isolated four submolecular proteins with molecular weights of 17,500, 37,400, 50,300, and 70,800.
  • Measured amino acid and carbohydrate contents showed similarities among the submolecular components and the whole thyroglobulin.
  • Sub. I exhibited significantly higher levels of thyroxine and triiodothyronine compared to the other components.

Cite This Study

Itagaki et al. (1978) studied this question.

synapsesocial.com/papers/69cd7ae65652765b073a87abhttps://doi.org/10.24517/00060081
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  1. 1Comprehensive proteomic and structural mapping of post-translational modifications of human thyroglobulin2026
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