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|Title:||Differential dissociation kinetics explain the binding preference of insulin-like growth factor binding protein-6 for insulin-like growth factor-II over insulin-like growth factor-I.|
|Authors:||Marinaro, J A;Jamieson, Gary P;Hogarth, P Mark;Bach, Leon A|
|Affiliation:||University of Melbourne, Department of Medicine, Austin and Repatriation Medical Centre, Heidelberg, Vic, Australia.|
|Citation:||Febs Letters; 450(3): 240-4|
|Abstract:||Insulin-like growth factor binding protein-6 binds insulin-like growth factor-II with a marked preferential affinity over insulin-like growth factor-I. The kinetic basis of this binding preference was studied using surface plasmon resonance. Binding of insulin-like growth factor-I and insulin-like growth factor-II to immobilized insulin-like growth factor binding protein-6 fitted a two-site binding kinetic model. Insulin-like growth factor-I and insulin-like growth factor-II association rates were similar whereas the dissociation rate was approximately 60-fold lower for insulin-like growth factor-II, resulting in a higher equilibrium binding affinity for insulin-like growth factor-II. The equilibrium binding affinities of a series of insulin-like growth factor-II mutants were also explained by differential dissociation kinetics. O-glycosylation had a small effect on the association kinetics of insulin-like growth factor binding protein-6. The insulin-like growth factor binding properties of insulin-like growth factor binding protein-6 are explained by differential dissociation kinetics.|
|Internal ID Number:||10359082|
Insulin-Like Growth Factor Binding Protein 6.metabolism
Insulin-Like Growth Factor I.metabolism
Insulin-Like Growth Factor II.metabolism
Recombinant Fusion Proteins.metabolism
Surface Plasmon Resonance
|Appears in Collections:||Journal articles|
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