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An Ex vivo Culture System to Study Thyroid Development
Published on: June 6, 2014
The subunits of thyroglobulin.
The Biochemical Journal
|March 1, 1970
Summary
Researchers reduced pig thyroglobulin using various agents, revealing reduction products around 165,000 molecular weight. Further analysis isolated two stable subunits of 35,000 and 20,000 molecular weight.
Area of Science:
- Biochemistry
- Protein Chemistry
Background:
- Thyroglobulin is a key protein in thyroid hormone synthesis.
- Understanding thyroglobulin structure is crucial for thyroid research.
Purpose of the Study:
- To investigate the subunit structure of pig thyroglobulin.
- To characterize the molecular weight of thyroglobulin reduction products.
Main Methods:
- Reduction of pig thyroglobulin using dithiothreitol in the presence of sodium dodecyl sulphate, 8M-urea, or 6M-guanidinium chloride.
- Separation of reduction products using Sephadex chromatography.
- Molecular weight determination of protein subunits.
Main Results:
- Pig thyroglobulin reduction yielded products with a molecular weight of approximately 165,000.
- Prolonged exposure to sodium dodecyl sulphate at pH 8.7 resulted in the separation of two stable subunits.
- The identified subunits had molecular weights of 35,000 and 20,000.
Conclusions:
- Pig thyroglobulin can be dissociated into smaller subunits under specific chemical conditions.
- A hydrolytic reaction is likely involved in the subunit dissociation, though the exact chemical linkages broken remain unidentified.
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