| 研究报告 |
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| 半胱氨酸蛋白酶IdeS的原核表达、纯化及活性鉴定 |
| 许静1, 赵自叶2, 徐进3,4, 郭怀祖3,4, 郑娟2, 段树燕2, 彭晓云5, 王皓1 |
1. 第二军医大学肿瘤研究所 上海 200433;
2. 聊城大学药学院 聊城 252000;
3. 上海交通大学药学院 上海 200240;
4. 抗体药物与靶向治疗国家重点实验室 上海 201203;
5. 华南理工大学生物科学与工程学院 广州 510006 |
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| Prokaryotic Expression,Purification and Activity Identification of Cysteine Hydrolase IdeS |
| XU Jing1, ZHAO Zi-ye2, XU Jin3,4, GUO Huai-zu3,4, ZHENG Juan2, DUAN Shu-yan2, PENG Xiao-yun5, WANG Hao1 |
1. Second Military Medical University, Shanghai 200433, China;
2. School of Pharmacy, Liaocheng University, Liaocheng 252000, China;
3. School of Pharmacy, Shanghai Jiaotong University, Shanghai 200240, China;
4. State Key Laboratory of Antibody Medicine and Targeted Therapy, Shanghai 201203, China;
5. School of Bioscience and Bioengineering, South China University of Technology, Guangzhou 510006, China |
引用本文:
许静, 赵自叶, 徐进, 郭怀祖, 郑娟, 段树燕, 彭晓云, 王皓. 半胱氨酸蛋白酶IdeS的原核表达、纯化及活性鉴定[J]. 中国生物工程杂志, 2014, 34(10): 8-14.
XU Jing, ZHAO Zi-ye, XU Jin, GUO Huai-zu, ZHENG Juan, DUAN Shu-yan, PENG Xiao-yun, WANG Hao. Prokaryotic Expression,Purification and Activity Identification of Cysteine Hydrolase IdeS. China Biotechnology, 2014, 34(10): 8-14.
链接本文:
https://manu60.magtech.com.cn/biotech/CN/10.13523/j.cb.20141002
或
https://manu60.magtech.com.cn/biotech/CN/Y2014/V34/I10/8
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[1] Wenig K, Chatwell L, von Pawel-Rammingen U, et al. Structure of the streptococcal endopeptidase IdeS, a cysteine proteinase with strict specificity for IgG. Proc Natl Acad Sci U S A, 2004, 101(50):17371-17376.
[2] Bisno A L, Stevens D L. Streptococcal infections of skin and soft tissues. N Engl J Med, 1996, 334(4):240-245.
[3] Lei B, DeLeo F R, Hoe N P, et al. Evasion of human innate and acquired immunity by a bacterial homolog of CD11b that inhibits opsonophagocytosis. Nat Med, 2001, 7(12):1298-1305.
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[7] Janin-Bussat M C, Tonini L, Huillet C, et al. Cetuximab Fab and Fc N-glycan fast characterization using IdeS digestion and liquid chromatography coupled to electrospray ionization mass spectrometry. Methods Mol Biol, 2013, 988:93-113.
[8] Vincents B, von Pawel-Rammingen U, Bjorck L, et al. Enzymatic characterization of the streptococcal endopeptidase, IdeS, reveals that it is a cysteine protease with strict specificity for IgG cleavage due to exosite binding. Biochemistry, 2004, 43(49):15540-15549.
[9] von Pawel-Rammingen U, Bjorck L. IdeS and SpeB: immunoglobulin-degrading cysteine proteinases of Streptococcus pyogenes. Curr Opin Microbiol, 2003, 6(1):50-55.
[10] Inouye K, Ohnaka S. Pepsin digestion of a mouse monoclonal antibody of IgG1 class formed F(ab')(2) fragments in which the light chains as well as the heavy chains were truncated. J Biochem Biophys Methods, 2001, 48(1):23-32.
[11] Lau H, Pace D, Yan B, et al. Investigation of degradation processes in IgG1 monoclonal antibodies by limited proteolysis coupled with weak cation-exchange HPLC. J Chromatogr B Analyt Technol Biomed Life Sci, 2010, 878(11-12):868-876.
[12] Johansson B P, Shannon O, Bjorck L. IdeS: a bacterial proteolytic enzyme with therapeutic potential. PLoS One, 2008, 3(2):e1692.
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