Abstract
AbstractThe three principal forces that govern the interaction between dissolved proteins and solid (flat or particulate) surfaces immersed in a polar liquid are:A. Lifshitz‐van der Waals forces (LW interactions)B. Polar (hydrogen bond, or Lewis acid‐base) forces (AB interactions, which include “hydrophobic” interactions)C. Electrostatic forces (EL interactions)EL interaction energies can be determined via electrokinetic measurements. LW and AB interaction energies are derived from the LW component and the electron‐acceptor (γ⊕) and electron‐donor (γ⊖) parameters of the AB component of the surface tension, all three of which can be determined by contact angle (Θ) measurements on (a) hydrated layers of protein and (b) flat layers of particulate surface, using at least 3 polar liquids in each case. By this approach, the optimal conditions for attachment as well as for detachment of a given protein to a well‐characterized solid surface or particle can be determined quantitatively. Reversed phase liquid chromatography of immunoglobulin G (1) on phenyl Sepharose (2) shows that the elution of the protein, by an increasing concentration of ethylene glycol (EG) in the aqueous medium (3), occurs at the EG concentration where the value of ΔG132TOT changes from negative to positive.
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
