摘要:
Type III TGF-β receptor is identified in and purified from normal human embryonic palatal mesenchyme (HEPM) cells and the purified product characterized structurally and functionally. HEPM cells were found to express high levels of the type III TGF-β receptor and were found to significantly down-regulate two classes of TGF-β receptor binding site. Purification of the type III TGF-β receptor from solubilized HEPM cell membranes by affinity chromatography yielded a biologically active protein of about 205 kd which specifically binds both the recombinant and natural forms of TGF-β1 and TGF-β2, with affinity dissociation constants in the picomolar range.
摘要:
Type III TGF-β receptor is identified in and purified from normal human embryonic palatal mesenchyme (HEPM) cells and the purified product characterized structurally and functionally. HEPM cells were found to express high levels of the type III TGF-β receptor and were found to significantly down-regulate two classes of TGF-β receptor binding site. Purification of the type III TGF-β receptor from solubilized HEPM cell membranes by affinity chromatography yielded a biologically active protein of about 205 kd which specifically binds both the recombinant and natural forms of TGF-β1 and TGF-β2, with affinity dissociation constants in the picomolar range.