Abstract
AbstractIt is shown that significant enhancements in the efficiency of protein recovery using reversed micelle extractants are possible if an affinity ligand surfactant is incorporated in the micellar phase formulation. The partitioning of the model protein concanavalin‐A was found to increase dramatically on addition of small amounts of octyl β‐D‐glucopyranoside (2 to 10 percent of the total surfactant concentration) to the organic reversed micellar phase, while transfer of ribonuclease‐A was essentially unaffected by the addition of this biological detergent. Glucose inhibited the solubilization of concanavalin‐A owing to competition for the binding sites between glucose and the affinity ligand. The experimental results were well described in terms of a simple thermodynamic model for the affinity partitioning of the protein between the two phases. Estimated binding constants for the protein‐ligand complex in the reversed micellar phase are consistent with published aqueous‐phase results.
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.
