Abstract
A novel combination of 2-D electrophoresis with hydrophobic partitioning in aqueous two-phase systems (ATPS) was extended to an alternative ATPS and both systems used for the three-dimensional characterization of the proteins extracted from soybeans. The 3-D plots of molecular weight, isoelectric point, and surface hydrophobicity were obtained using two different phase-forming salts: Na2SO4 and potassium phosphate. Six proteins with known hydrophobicities were used to validate the ATPS-based method. Molecular properties obtained using the PEG-sulfate system resulted in a wider range of proteins characterized. The wide range of concentration and strongly hydrophilic character of the soy extracts limited the coverage obtained; reduction of the storage protein content aided detection. The number of proteins simultaneously and accurately characterized by this method as currently implemented is limited by the dynamic range of staining, the ability to quantify strongly partitioning proteins in both phases, and loss of proteins of limited solubility in the ATPS or during the removal of phase-forming components.
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.
