Please use this identifier to cite or link to this item: http://hdl.handle.net/10397/9822
Title: Effect of receptor phosphorylation on the binding between IRS-1 and IGF-1R as revealed by surface plasmon resonance biosensor
Authors: Huang, M
Lai, WP
Wong, MS 
Yang, M
Keywords: Biosensor
Insulin receptor substrate-1
Insulin-like growth factor-1 receptor
Surface plasmon resonance
Tyrosine phosphorylation
Issue Date: 2001
Publisher: Elsevier Science Bv
Source: FEBS letters, 2001, v. 505, no. 1, p. 31-36 How to cite?
Journal: FEBS Letters 
Abstract: A receptor binding assay based on the surface plasmon resonance (SPR) biosensor technique was developed to study the interaction between insulin-like growth factor-1 receptor (IGF-1R) and its intracellular substrate protein insulin receptor substrate-1 (IRS-1). The sensor surface was modified with anti-IGF-1R (α-subunit) monoclonal antibodies for the capturing of the receptor-containing membrane fragments from cell lysates. The IGF-1R was successfully immobilized on the sensor surface with binding capability for its intracellular substrates. SPR measurements showed that the tyrosine phosphorylation of IGF-1R induced by its extracellular ligand insulin-like growth factor-1 caused the receptor to bind with IRS-1 10 times faster than the unactivated receptor. As a result, the affinity constants of IRS-1 to phosphorylated and unphosphorylated IGF-1R were (8.06 ± 5.18) × 109 M-1 and (9.81 ± 4.61) × 108 M-1, respectively.
URI: http://hdl.handle.net/10397/9822
ISSN: 0014-5793
DOI: 10.1016/S0014-5793(01)02780-6
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