| 초록 |
In this study, using recombinant human growth hormone as a model protein, we carried out unfolding by adding a denaturant such as urea, guanidine HCl, or SDS followed by refolding by dilution or dialysis. The objectives were to compare the refolding performance of each denaturant and to investigate the kinetics of refolding. The changes in surface hydrophobicity were measured by fluorescence tagging of 1-anilinonaphthalene-8-sulfonate (1, 8-ANS) to the hydrophobic portions. The changes in the secondary structure were monitored by using far UV-CD (circular dichroism) spectroscopy. Also, we used RP-HPLC to separate and quantify the folded and unfolded proteins to correlate the result with the structure analysis.
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