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Self-association studies on the EphB2 receptor SAM domain using analytical ultracentrifugation

Item Type:Article
Title:Self-association studies on the EphB2 receptor SAM domain using analytical ultracentrifugation
Creators Name:Behlke, J. and Labudde, D. and Ristau, O.
Abstract:The self-association behavior of the Eph-kinases SAM domain has been studied in phosphate buffer, pH 7.4, containing 0.14 M NaCl using concentration-dependent sedimentation equilibrium experiments. Only weak interactions typical for a monomer-dimer equilibrium up to at least 12 mg/mL were observed. Such concentrated solutions require a consideration of the non-ideality expressed by virial coefficients. A special centrifuge equation was used for the global analysis to estimate equilibrium constants based on the thermodynamic activities of the reactants. When neglecting this, the parameters deviate by about 20%. Association constants for dimerization of the EphB2-SAM domain vary between 163 M-1 at 10 °C and 395 M-1 at 32 °C, indicating hydrophobic forces are involved in the dimerization process. In solutions of about 12 mg/mL, less than 50% dimers are in solution and higher oligomers can be excluded.
Keywords:Analytical Ultracentrifugation, EphB2 Receptor SAM, Self-Association, Virial Coefficients
Source:European Biophysics Journal with Biophysics Letters
Page Range:411-415
Date:1 January 2001
Official Publication:https://doi.org/10.1007/s002490100164
PubMed:View item in PubMed

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