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Buffalo thyroglobulin.

V Deshpande1

  • 1Department of Biochemistry, University College of Science, Osmania University, Andhra Pradesh, India.

Comparative Biochemistry and Physiology. B, Comparative Biochemistry
|January 1, 1991
PubMed
Summary
This summary is machine-generated.

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Buffalo thyroglobulin, a major iodoprotein, is rich in iodine and distinct in its amino acid composition and N-terminal residue compared to other mammals. Its structure comprises eight non-identical subunits.

Area of Science:

  • Biochemistry
  • Endocrinology
  • Proteomics

Background:

  • Thyroglobulin is the primary iodoprotein in mammalian thyroid glands, crucial for thyroid hormone synthesis.
  • Variations in thyroglobulin structure and composition exist across species, influencing hormone production and iodine metabolism.

Purpose of the Study:

  • To characterize the biochemical and structural properties of buffalo thyroglobulin.
  • To compare buffalo thyroglobulin with thyroglobulins from other mammalian species.

Main Methods:

  • Ultracentrifugation to determine sedimentation coefficient and molecular mass.
  • Chemical analysis for iodine content, carbohydrate composition, and amino acid profiling.
  • N-terminal amino acid sequencing and quaternary structure analysis.

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Main Results:

  • Buffalo thyroglobulin exhibits a sedimentation coefficient of 19 S and a molecular mass of 685 kDa.
  • The protein is notably rich in iodine (1-2%) and thyroxine-bound iodine (75%), with 8.41-9.61% carbohydrate content.
  • It contains 2% more proline and exclusively glutamic acid as the N-terminal amino acid, differing from other species; its quaternary structure consists of eight non-identical subunits.

Conclusions:

  • Buffalo thyroglobulin possesses unique biochemical and structural characteristics, particularly its high iodine content and distinct N-terminal residue.
  • These unique features may play a role in the specific thyroid hormone metabolism or iodine handling in buffaloes.