Characterization of unique binding kinetics of follistatin and activin or inhibin in serum
作者： A L Schneyer , D A Rzucidlo , P M Sluss , W F Crowley
DOI: 10.1210/ENDO.135.2.8033815
关键词: Follistatin 、 Activin and inhibin 、 Biology 、 Peptide hormone 、 Receptor 、 Endocrinology 、 Activin binding 、 Receptor–ligand kinetics 、 Internal medicine 、 Binding protein 、 Size-exclusion chromatography
摘要: Serum binding proteins (BPs) have been identified for several peptide and protein hormones, their presence has significant implications the biological action of hormone. Follistatin (FS) as an activin- inhibin-BP in tissues, serum, follicular fluid species, including humans. In this study, kinetics FS activin inhibin were characterized human serum using gel filtration chromatography compared to those pure recombinant hormones a new solid phase assay. When complexed with radiolabeled or inhibin, eluted at volume corresponding mol wt range 67,000-150,000, elution identical lower BP peak observed serum. Furthermore, kinetic analyses assay revealed that 1) FS-activin interaction is high affinity, similar exceeding estimated its receptor; 2) activin...
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