Molecular Aspects of the Subunit Assembly of Glycoprotein Hormones

  • Jean Garnier
Part of the Biochemical Endocrinology book series (BIOEND)


The understanding of the molecular basis of gonadotropin hormone action requires a knowledge of the structural properties of the hormones Amino acid sequence analyses (see reviews in Wallis, 1975; Pierce et al., 1976; Dayhoff, 1976) have shown that gonadotropins and thyrotropin (TSH) share a common subunit of 89–96 amino acid residues with five disulfide bonds, designated α. The other subunit (ß) is chemically different, although related, for each hormone and contains six disulfide bonds for 116–147 amino acid residues.


Circular Dichroism Luteinizing Hormone Disulfide Bond Tyrosine Residue Human Chorionic Gonadotropin 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

Abbreviations used in this chapter

b, c, h, o, s

letter prefixes denoting, respectively bovine, carp, human, ovine, and salmon hormones


1,8-anilinonaphthalene sulfonate


circular dichroism


fish gonadotropin


follitropin (follicle-stimulating hormone)


human choriogonadotropin


lutropin (luteinizing hormone)


thyrotropin (thyroid-stimulating hormone)


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Copyright information

© Plenum Press, New York 1978

Authors and Affiliations

  • Jean Garnier
    • 1
  1. 1.Laboratoire de Biochimie physique, I.N.R.AUniversité de Paris-SudOrsayFrance

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