Please use this identifier to cite or link to this item: http://ahro.austin.org.au/austinjspui/handle/1/9161
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.
Issue Date: 7-May-1999
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
URI: http://ahro.austin.org.au/austinjspui/handle/1/9161
URL: http://www.ncbi.nlm.nih.gov/pubmed/10359082
Type: Journal Article
Subjects: Binding, Competitive
Cell Line
Glycosylation
Humans
Insulin-Like Growth Factor Binding Protein 6.metabolism
Insulin-Like Growth Factor I.metabolism
Insulin-Like Growth Factor II.metabolism
Kinetics
Recombinant Fusion Proteins.metabolism
Solutions
Surface Plasmon Resonance
Appears in Collections:Journal articles

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