scholarly journals The rat ovarian lutropin receptor. Purification, hormone binding properties, and subunit composition.

1986 ◽  
Vol 261 (20) ◽  
pp. 9450-9460 ◽  
Author(s):  
R C Bruch ◽  
N R Thotakura ◽  
O P Bahl
Keyword(s):  
Subunit Composition ◽  
Hormone Binding ◽  
Binding Properties ◽  
Receptor Purification ◽  
Lutropin Receptor

scholarly journals Effect of deglycosylation on the structure and hormone-binding activity of the lutropin receptor

1988 ◽  
Vol 256 (3) ◽  
pp. 719-724 ◽  
Author(s):  
K P Keinänen
Keyword(s):  
Polyacrylamide Gel Electrophoresis ◽  
Binding Activity ◽  
Hormone Binding ◽  
Binding Properties ◽  
Lh Receptor ◽  
High Affinity ◽  
Human Choriogonadotropin ◽  
Lutropin Receptor ◽  
Membrane Bound ◽  
Polypeptide Backbone

Affinity-purified rat ovarian lutropin (LH) receptor is a single 90 kDa polypeptide which binds to immobilized lectins, indicating that the receptor is a glycoprotein [Keinänen, Kellokumpu, Metsikkö & Rajaniemi (1987) J. Biol. Chem. 262, 7920-7926]. In the present study the glycoprotein nature of the rat ovarian LH receptor was investigated in order to determine the contribution of the glycan moiety to receptor's size and hormone-binding properties. Treatment of the 125I-labelled purified LH receptor with neuraminidase and peptide N-glycosidase F resulted in a decrease in size of LH receptor from 90 kDa to 79 kDa and 62 kDa respectively, as assessed by SDS/polyacrylamide-gel electrophoresis. Endo-alpha-N-acetylgalactosaminidase treatment did not affect the electrophoretic mobility of the intact or neuraminidase-treated LH receptor. Subjecting the membrane-bound LH receptor to similar enzymic treatments followed by ligand blotting showed that the 79 kDa and 62 kDa forms are capable of specific hormone binding. Furthermore, intact and peptide N-glycosidase F-treated membranes bound 125I-labelled human choriogonadotropin with similar affinities. These data suggest that molecular mass of the polypeptide backbone of the LH receptor is 62 kDa. The receptor contains N-glycosidically linked oligosaccharide chains with terminal sialic acid residues, with little or no O-linked oligosaccharide. N-Linked carbohydrate is not required for specific high-affinity hormone binding.

Lymphocyte glucocorticoid receptor expression level and hormone-binding properties differ between war trauma-exposed men with and without PTSD

2013 ◽  
Vol 43 ◽  
pp. 238-245 ◽  
Author(s):  
Gordana Matić ◽  
Danijela Vojnović Milutinović ◽  
Jelena Nestorov ◽  
Ivana Elaković ◽  
Sanja Manitašević Jovanović ◽  
...  
Keyword(s):  
Glucocorticoid Receptor ◽  
War Trauma ◽  
Receptor Expression ◽  
Expression Level ◽  
Hormone Binding ◽  
Binding Properties
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