Abstract:
: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.
journal_name
Proc Natl Acad Sci U S Aauthors
Ramasharma K,Li CHdoi
10.1073/pnas.84.11.3595subject
Has Abstractpub_date
1987-06-01 00:00:00pages
3595-8issue
11eissn
0027-8424issn
1091-6490journal_volume
84pub_type
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