Mechanisms and Regulation of TSH Glycosylation

  • Neil Gesundheit
  • Bruce D. Weintraub
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 205)


Thyroid-stimulating hormone (TSH) is a glycoprotein composed of two noncovalently linked subunits, α and β. The structure of TSH from a variety of species has been well characterized, including the amino acid sequence and carbohydrate composition (Pierce and Parsons, 1981). The α-subunit of bovine TSH has a molecular weight of 13,600, of which 10,800 is composed of a protein core of 96 amino acids and 2,800 (21%) represents two oligosaccharide units linked to asparagine residues. Bovine TSH-β has a molecular weight of 14,700, of which 13,100 is comprised of a protein core of 113 amino acids and 1,600 (12%) represents one asparagine-linked oligosaccharide unit.


Sialic Acid Rough Endoplasmic Reticulum High Mannose Subunit Combination Oligosaccharide Moiety 
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Copyright information

© Plenum Press, New York 1986

Authors and Affiliations

  • Neil Gesundheit
    • 1
    • 2
  • Bruce D. Weintraub
    • 1
    • 2
  1. 1.Molecular, Cellular and Nutritional Endocrinology BranchNational Institute of Arthritis, DiabetesBethesdaUSA
  2. 2.Digestive and Kidney DiseasesNational Institutes of HealthBethesdaUSA

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