Abstract:
:The IGF-I receptor binds IGF-I with complex kinetics characterized by a curvilinear Scatchard plot, suggesting receptor heterogeneity and apparent negative cooperativity. To explore the molecular mechanisms underlying these properties, we have characterized the binding of a hybrid receptor formed from a wild-type receptor monomer and a mutant receptor monomer devoid of binding activity. Receptor hybrids were generated by transient co-transfection of cDNAs encoding wild-type and mutant receptors with unique epitope tags. Hybrid receptors were purified from transfected cells by sequential immuno-affinity chromatography and their ligand-binding properties were determined. Complementation produced a hybrid with near wild-type affinity. Dissociation studies demonstrated that the hybrid did not exhibit negative cooperativity.
journal_name
Biochem Biophys Res Communjournal_title
Biochemical and biophysical research communicationsauthors
Chakravarty A,Hinrichsen J,Whittaker L,Whittaker Jdoi
10.1016/j.bbrc.2005.03.122subject
Has Abstractpub_date
2005-05-27 00:00:00pages
74-7issue
1eissn
0006-291Xissn
1090-2104pii
S0006-291X(05)00641-8journal_volume
331pub_type
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journal_title:Biochemical and biophysical research communications
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