| Proteins are the basis of living bodies and important part of biological cells, which owns close relationships to various life activities. As a kind of biological macromolecules with bioactivities, proteins generally have poor stabilities and tend to undergo conformational change in the process of purification, therefore, the development of mild and efficient extraction methods for the isolation of protein from complex sample matrixes become a key issue in proteomics and protein engineering.In this thesis, Keggin-type phosphomolybdates, e.g., (C19H42N)3PMo12O40, are prepared by solid-state chemical reaction and liquid phase method at room temperature, respectively. The as-prepared phosphomolybdates are thus characterized by means of thermal gravity analysis, scanning electron microscope, Fourier transform infrared spectroscopy, X-ray diffraction and elemental analysis. Porous products are obtained by solid-state method. The performances of the obtained phosphomolybdate in the separation/purification of proteins are studied and the experimental results indictae that selective adsorption of hemoglobin could be achieved by using this phosphomolybdate as sorbent. Under pH 6.0, an adsorption of 91.4% for 100 mg L-1 hemoglobin in a 1.0 mL solution is achieved by using 5.0 mg of phosphomolybdate with a sorption time of 20 min. The adsorption of hemoglobin onto phosphomolybdate fits Langmuir adsorption model, corresponding to a theoretical adsorption capacity of 55.86 mg g-1. The adsorbed hemoglobin could be readily stripped by imidazole-HCl solution of pH 7.0, giving rise to an elution efficiency of 64.7%. A solid-phase extraction protocol is thus developed for the isolation of hemoglobin from human blood and the results of sodium dodecyl sulfate polyacrylamide gel electrophoresis suggest that hemoglobin of high purity is obtained.The experimental results illustrate the great application potentials of polyoxometalates in the field of life science applications. |
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