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N-terminal groups of buffalo thyroglobulin.
V Deshpande1, L K Ramachandran
1Department of Biochemistry, Osmania University, Hyderabad.
Indian Journal of Biochemistry & Biophysics
|April 1, 1990
Summary
Buffalo thyroglobulin
Area of Science:
- Biochemistry
- Proteomics
- Endocrinology
Background:
- Thyroglobulin is a key protein in thyroid hormone synthesis.
- Understanding thyroglobulin's N-terminal structure is crucial for its function.
- Mammalian thyroglobulin N-terminals vary, impacting protein processing.
Purpose of the Study:
- To determine the N-terminal amino acid of buffalo thyroglobulin.
- To compare buffalo thyroglobulin's N-terminus with other mammalian counterparts.
Main Methods:
- N-terminal analysis using Sanger's fluorodinitrobenzene method.
- Confirmation via Edman degradation and phenylthiohydantoin (PTH)-amino acid characterization.
Main Results:
- Glutamic acid was identified as the N-terminal amino acid of buffalo thyroglobulin.
- Approximately 1.5 moles of DNP-glutamic acid were found per mole of thyroglobulin.
- No water-soluble N-terminal DNP-amino acids were detected.
Conclusions:
- Buffalo thyroglobulin uniquely features glutamic acid at its N-terminus.
- This contrasts with aspartic acid or asparagine found in other mammalian thyroglobulins.
- The N-terminal composition may influence thyroglobulin's biological role.