Zoological origin of gonadotropin subunits and association kinetics
- 1 September 1979
- journal article
- Published by Springer Nature in Nature
- Vol. 281 (5729) , 314-315
- https://doi.org/10.1038/281314a0
Abstract
Mammalian luteinizing hormone (LH) is an association of two dissimilar subunits, alpha and beta. In vitro studies, mainly using difference spectrophotometry, had shown that this phenomenon was slow, especially at low temperatures. If the situation was the same in poikiloterms, it would probably make gonadotropin (GTH) synthesis difficult for these animals in a cold environment. We have found that the formation of a teleost gonadotropin is in fact strikingly more rapid and less thermodependent than formation of mammalian LH. Also, studies with a fish-mammal hybrid molecule have allowed us to estimate the respective influence of the alpha and beta subunits in determining these differences.Keywords
This publication has 8 references indexed in Scilit:
- The evolution of gonadotropins: some molecular data concerning a non-mammalian pituitary gonadotropin, the hormone from a teleost fish (Cyprinus carpio L.)Biochimie, 1978
- Molecular Aspects of the Subunit Assembly of Glycoprotein HormonesPublished by Springer Nature ,1978
- Biochemical and Biological Properties of Fish Gonadotropins and Their Subunits: Comparison with Mammalian HormonesPublished by Springer Nature ,1978
- In vitro activation of glycoprotein hormones Hybridization of subunits from thyrotropin, lutropin and human choriogonadotropinBiochimica et Biophysica Acta (BBA) - Protein Structure, 1976
- Association-dependent active folding of alpha and beta subunits of lutropin (luteinizing hormone)Journal of Molecular Biology, 1975
- The rates of dissociation and recombination of the subunits of human luteinizing hormoneArchives of Biochemistry and Biophysics, 1973
- Structural modifications involved in the dissociation and reassociation of the α and β subunits of ovine luteinizing hormoneFEBS Letters, 1971
- Reversible dissociation into subunits and biological activity of ovine luteinizing hormoneBiochimica et Biophysica Acta (BBA) - Protein Structure, 1969