影响重组凝乳酶原再折叠的主要原因研究

影响重组凝乳酶原再折叠的主要原因研究 SCRAMBLED DISULFIDE BONDS UNFAVOUR THE CORRECT REFOLDING OF RECOMBINANT PROCHYMOSIN 唐兵 Tang Bing 1 first-author 武汉大学生命科学学院 武汉大学生命科学学院 College of Life Sciences, Wuhan University College of Life Sciences, Wuhan University 对蛋白质二硫键异构酶与ＧＳＨ／ＧＳＳＧ促进重组凝乳酶原复性进行了比较．ＧＳＨ／ＧＳＳＧ促进重组凝乳酶原复性的效率低于蛋白质二硫键异构酶，但最终效果相似．ＧＳＨ／ＧＳＳＧ与蛋白质二硫键异构酶促进重组凝乳酶原复性的反应没有叠加效应．在低蛋白浓度条件下进行复性时，二硫键的错误配对是影响重组凝乳酶原再折叠的主要原因． By comparing PDI assisted renaturation with GSH/GSSG assisted renaturation of recombinant prochymosin, we found that: （1）Although the reaction rate of GSH/GSSG assisted renaturation was lower than that of PDI assisted renaturation, there was no difference between the final renaturation efficiencies of them. （2） No cumulative effect was detected in the renaturation assisted with PDI and GSH/GSSG. （3） Under the renaturation condition described here, there was no aggregation resulted from high protein concentration. Based on these results, we proposed that scrambled disulfide bond unfavoured the correct refolding of recombinant prochymosin and the correct pairing of native disulfide bonds faciliated the formation of native prochymosin. 重组凝乳酶原 再折叠 二硫键 recombinant prochymosin refolding disulfide bond Q556.1 国家863高技术项目 1997-06-01 2021-04-01 6