| 脯氨酰顺－反异构酶的纯化及对重组蛋白质折叠反应的催化性能 |
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| 引用本文： | 徐明波,孟文华,马贤凯. 脯氨酰顺－反异构酶的纯化及对重组蛋白质折叠反应的催化性能[J]. 生物化学与生物物理进展, 1994, 21(3): 247-251 |
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| 作者姓名： | 徐明波 孟文华 马贤凯 |
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| 作者单位： | 军事医学科学院基础医学研究所;军事医学科学院基础医学研究所;军事医学科学院基础医学研究所 |
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| 基金项目： | “863”项目的一部分. |
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| 摘 要： | 脯氨酰异构是蛋白质折叠反应的限速步骤之一，体内被脯氨酰顺－反异构酶(PPI)所催化．为了研究PPI在重组蛋白体外折叠复性中的作用，我们自猪肾脏中纯化了PPI，并对重组蛋白的酶促折叠过程进行了探讨．结果表明，PPI催化的重组蛋白的折叠反应主要是提高了它们的折叠速率，而不增加正确折叠率和比活性，PPI在很低的浓度下即有很高的催化活性．
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| 关 键 词： | 重组蛋白 折叠 脯氨酰顺－反异构酶 |
| 收稿时间： | 1993-05-07 |
| 修稿时间： | 1993-08-23 |
Studies on the Purification of PPI and its Catalyzing Activity for Folding of Recombinant Proteins |
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| Xu Mingbo,Meng Wenhua and Ma Xiankai. Studies on the Purification of PPI and its Catalyzing Activity for Folding of Recombinant Proteins[J]. Progress In Biochemistry and Biophysics, 1994, 21(3): 247-251 |
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| Authors: | Xu Mingbo Meng Wenhua Ma Xiankai |
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| Affiliation: | Institute of Basic Medical Sciences, P.O.Box 130-3;Institute of Basic Medical Sciences, P.O.Box 130-3;Institute of Basic Medical Sciences, P.O.Box 130-3 |
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| Abstract: | Proline isomerization catalyzed by peptidyl-prolyl cis-trans isomerase (PPI) in vivo is a limited procedure in protein folding. In order to study the catalyzing activity of PPI on the refolding of recombinant proteins in vitro,PPI is purified from pig kidney.and is investigated the effects of the enzyme on catalyzing the refolding process. Results indicate that PPI increases the folding rate without increasing the correct folding ratio and specific activity.and PPI has a high catalyzing activity even at very low concentration. |
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| Keywords: | recombinant protein refolding PPI |
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