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THE MOLECULAR WEIGHT AND ISOELECTRIC POINT OF THYROGLOBULIN
1Institute for Physical Chemistry of the University of Upsala, Sweden, the Department of Medicine, College of Physicians and Surgeons, Columbia University, and the Presbyterian Hospital, New York.
The Journal of General Physiology
|October 30, 2009
Summary
Hog thyroglobulin shares similar sedimentation properties with human thyroglobulin. Its molecular weight is approximately 700,000, and the molecule is non-spherical, indicating complex structural characteristics.
Area of Science:
- Biochemistry
- Molecular Biology
- Protein Chemistry
Background:
- Thyroglobulin is a key protein in thyroid hormone synthesis.
- Understanding thyroglobulin's biophysical properties is crucial for thyroid research.
Purpose of the Study:
- To characterize the biophysical properties of hog thyroglobulin.
- To compare these properties with human thyroglobulin.
Main Methods:
- Sedimentation velocity and equilibrium ultracentrifugation.
- Isoelectric focusing.
- Specific volume measurements.
Main Results:
- Hog thyroglobulin sedimentation constant: 19.2 x 10^-13 s.
- Specific volume: 0.72 cm^3/g.
- Isoelectric point (native): pH 4.58; (denatured): pH 5.0.
- Molecular weight: ~700,000 (sedimentation-diffusion), ~650,000 (sedimentation equilibrium).
- Thyroglobulin molecule is non-spherical.
Conclusions:
- Hog and human thyroglobulin exhibit similar sedimentation behavior.
- The molecular weight and non-spherical shape provide insights into thyroglobulin structure.
- These findings contribute to the understanding of thyroid protein characteristics.
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