title: Characterization of activin A binding sites on the human leukemia cell line K562.
abstract: Recombinant activin A was radioiodinated to a high specific activity with maintenance of bioactivity using the Bolton-Hunter method. The human leukemia cell line K562, known to differentiate in response to activin A, was found to possess high affinity [125I]BH-activin A receptors (Kd approximately 0.13 nM) with a low number of receptors per cell (approximately 600 per cell). This receptor was found to be specific as FSH, LH, GnRH, and TGF-beta 1 do not compete for binding. This is the first description of binding sites for this protein hormone on K562 cells.
authors.affiliation: Clayton Foundation Laboratories for Peptide Biology, Salk Institute, La Jolla, California 92037.
authors.forename: C A
authors.initials: CA
authors.lastname: Campen
authors.forename: W
authors.initials: W
authors.lastname: Vale
mesh_terms: D028341:Activins; D001667:Binding, Competitive; D006801:Humans; D007265:Inhibins / Q000378:metabolism*; D007700:Kinetics; D004915:Leukemia, Erythroblastic, Acute / Q000378:metabolism*; D008970:Molecular Weight; D011869:Radioligand Assay; D011994:Recombinant Proteins; D013329:Structure-Activity Relationship; D013696:Temperature; D014407:Tumor Cells, Cultured
chemical_list: D011994:Recombinant Proteins; D028341:Activins; D007265:Inhibins