Identification, characterization, and stabilization of the deamidation degradation of recombinant human tumor necrosis factor-α

详细信息    查看全文

• 作者：Shuang Yin^a ; ^b ; ¹ ; Chun Zhang^a ; ^b ; ¹ ; Zenglan Li^b ; Qi Wang^b ; Hong Shi^b ; Rong Yu^a ; ^{yurong@scu.edu.cn} ; Yongdong Liu^b ; ^{ydliu@ipe.ac.cn} ; Zhiguo Su^b
• 关键词：rhTNF-α ; recombinant human tumor necrosis factor ; LC&ndash ; MS/MS ; liquid chromatography coupled with tandem mass spectrometry ; HP-SEC ; high-performance size-exclusion chromatography ; CD ; circular dichroism ; FL ; fluorescence spectrometry ; Asn(N) ; asparagine ; Gln(Q) ; glutamine ; Asp(D) ; aspartic acid ; SAX-HPLC ; strong anion exchange high-performance liquid chromatography ; UV ; ultraviolet&ndash ; visible ; PAGE ; polyacrylamide gel electrophoresis ; SDS ; sodium dodecyl sulfonate ; ACN ; acetonitrile ; EDTA
• 刊名：Process Biochemistry
• 出版年：2017
• 出版时间：February 2017
• 年：2017
• 卷：53
• 期：Complete
• 页码：216-223
• 全文大小：1796 K
• 卷排序：53

文摘

The Asp34 and Asp 39 residues are found to deamidate in tumor necrosis factor-α. Asp34 deamidation causes notable decrease of bioactivity of tumor necrosis factor-α. Glycerol has a good capacity for retarding deamidation.