Publication Date:
1985-07-05
Description:
The biological properties of recombinants of glycoprotein hormones in which the alpha and beta subunits were differentially deglycosylated have been investigated. Specific deglycosylation of the alpha subunit generated a recombinant that had more receptor-binding activity but did not produce hormone response in the target cells. The deglycosylated alpha + beta recombinant was also an antagonist of the action of the native hormone. Thus, the carbohydrates in the alpha subunit play a dominant role in the transduction of the hormone signal into the cell.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sairam, M R -- Bhargavi, G N -- New York, N.Y. -- Science. 1985 Jul 5;229(4708):65-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2990039" target="_blank"〉PubMed〈/a〉
Keywords:
Animals
;
Cyclic AMP/metabolism
;
Female
;
Follicle Stimulating Hormone/*physiology
;
Glycoproteins/*physiology
;
Leydig Cells/physiology
;
Luteinizing Hormone/*physiology
;
Male
;
Ovary/physiology
;
Rats
;
Receptors, Cell Surface/*physiology
;
Receptors, FSH
;
Receptors, LH
;
Seminiferous Tubules/physiology
;
Sheep
;
Structure-Activity Relationship
;
Swine
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
