作者: Joe A. Marinaro , Gary P. Jamieson , P.Mark Hogarth , Leon A. Bach
DOI: 10.1016/S0014-5793(99)00499-8
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摘要: Insulin-like growth factor binding protein-6 binds insulin-like factor-II with a marked preferential affinity over factor-I. The kinetic basis of this preference was studied using surface plasmon resonance. Binding factor-I and to immobilized fitted two-site model. association rates were similar whereas the dissociation rate ∼60-fold lower for factor-II, resulting in higher equilibrium factor-II. affinities series mutants also explained by differential kinetics. O-glycosylation had small effect on kinetics protein-6. properties are