Characteristics of binding of human seminal alpha-inhibin-92 to human pituitary membranes.
AUTOR(ES)
Ramasharma, K
RESUMO
We investigated the binding of 125I-labeled alpha-inhibin-92 (a 92-residue peptide) to human pituitary membrane preparations. Unlabeled alpha-inhibin-92 competed effectively with the labeled peptide for binding to the membranes. Binding was also inhibited by both alpha-inhibin-52 and alpha-inhibin-31, but less effectively. Scatchard analysis of the alpha-inhibin-92 binding data indicated the presence of high-affinity binding sites (1.35 nM/mg of membrane protein) with an apparent Kd of 0.37 nM. When 125I-labeled alpha-inhibin-92 was covalently crosslinked to the pituitary membrane preparation with disuccinimidyl suberate and the solubilized labeled receptor complex was analyzed by NaDodSO4/PAGE under either reducing or nonreducing conditions, a single radioactive band at an apparent molecular weight of 90,000 +/- 5000 was observed. These data suggest that human pituitary has specific binding sites for alpha-inhibins.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=304921Documentos Relacionados
- Synthetic human seminal alpha-inhibin-92 selectively suppresses follicle-stimulating hormone release in vivo.
- Synthetic human seminal α-inhibin-92 selectively suppresses follicle-stimulating hormone release in vivo
- Specific binding of human corticosteroid-binding globulin to cell membranes.
- Characterization of high density lipoprotein binding to human adipocyte plasma membranes.
- Binding of lipoteichoic acid of group A streptococci to isolated human erythrocyte membranes.
