Extensive Imprinting Adaptability of Polyacrylamide-based Amphoteric Cryogels Against Protein Molecules / 分析化学

Lysozyme, pepsin, ovalbumin, hemoglobin andγ-globumin were chosen as templates to investigate the imprinting capability of amphoteric polyacrylamide cryogels. Prepolymerizing solutions contained acrylic acid and allyl amine, as well as acrylamide and N,N'-methylenebisacrylamide as the functional monomers. As a result there were both acidic and basic functional groups in the polymers, facilitating effective interactions with likewise amphoteric proteins. The proteins differ greatly and cover wide scopes of molecular weights and isoelectric points. Regardless of the values of the molecular weights and isoelectric points, all the templates gave higher retentions on the MIP tubes than on the NIP tube. The MIP of lysozyme indicated the highest imprinting factor of 7. 0, and that of γ-globumin showed the lowest, 2. 0. The values of other proteins were intervenient. Conclusively the amphoteric polyacrylamide cryogels were suitable imprinting materials for various proteins, and could potentially be used for protein recognition, purification, and depletion.

Depletion of Chicken Egg White Proteins by Pending Templates Imprinted Polymers / 分析化学

Eggwhitesolutionswereusedas“pendingtemplates”topreparemolecularimprintedpolymers. The obtained polymers acted as stationary phases, exhibiting abilities to deplete abundant proteins in the egg white. The abilities of protein depletion of the imprinted polymers could be adjusted by using different concentrations of egg white in preparing the polymers. After chromatographically processed in a home-made syringe system, abundant proteins such as ovalbumin, lysozyme, and ovotransferrin were removed from egg white sample solutions. Along with the disappearance of the mass spectrum peaks of these proteins, the signals of other components became more obvious. Meanwhile according to reference data and molecular weights, they were reasonably ascribed to be ovalbumin-related proteins, ovotransferrin-related proteins, ovomucoids or flavoproteins respectively. Conclusively, pending imprinting method has the power to deplete abundant proteins, and to retain and enrich posttranslationally modified species at the same time.