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Quantitatively investigating monomethoxypolyethylene glycol modification of protein by capillary electrophoresis
Alternative TitleJ. Biochem. Biophys. Methods
Li, WJ; Su, ZG
2004-04-30
Source PublicationJOURNAL OF BIOCHEMICAL AND BIOPHYSICAL METHODS
ISSN0165-022X
Volume59Issue:1Pages:65-74
AbstractCapillary electrophoresis (CE) was applied to study quantitatively protein modification with succinimidyl succinate-activated monomethoxypolyethylene glycol (MPEG-SS). The heterogeneous distribution of modified proteins and the average modification degree were determined by CE, and the latter met with the results from 2,4,6-trinitrobenzenesulfonic acid (TNBS) spectrometric assay. It was found that the optimal buffer pH for the modification was between pH 7.4 and 8.4, and the modification degree decreased when the modified sample was preserved in high pH solutions. The protein fractions attached with different number of polyethylene glycols (PEGs) were monitored along the process of protein modification. CE was proved to be efficient to evaluate quantitatively several factors of the protein modification, including the modifier/protein molar ratio, the stability of conjugates in different pH environments, and the time course of modification process. (C) 2003 Published by Elsevier B.V.; Capillary electrophoresis (CE) was applied to study quantitatively protein modification with succinimidyl succinate-activated monomethoxypolyethylene glycol (MPEG-SS). The heterogeneous distribution of modified proteins and the average modification degree were determined by CE, and the latter met with the results from 2,4,6-trinitrobenzenesulfonic acid (TNBS) spectrometric assay. It was found that the optimal buffer pH for the modification was between pH 7.4 and 8.4, and the modification degree decreased when the modified sample was preserved in high pH solutions. The protein fractions attached with different number of polyethylene glycols (PEGs) were monitored along the process of protein modification. CE was proved to be efficient to evaluate quantitatively several factors of the protein modification, including the modifier/protein molar ratio, the stability of conjugates in different pH environments, and the time course of modification process. (C) 2003 Published by Elsevier B.V.
KeywordCapillary Electrophoresis Chemical Modification Polyethylene Glycol Protein
SubtypeArticle
WOS HeadingsScience & Technology ; Life Sciences & Biomedicine
DOI10.1016/j.jbbm.2003.11.004
URL查看原文
Indexed BySCI
Language英语
WOS KeywordMODIFIED SUPEROXIDE-DISMUTASE ; POLYETHYLENE-GLYCOL ; RIBONUCLEASE ; DERIVATIVES ; AMINES
WOS Research AreaBiochemistry & Molecular Biology ; Biophysics
WOS SubjectBiochemical Research Methods ; Biochemistry & Molecular Biology ; Biophysics
WOS IDWOS:000221684800004
Citation statistics
Cited Times:5[WOS]   [WOS Record]     [Related Records in WOS]
Document Type期刊论文
Version出版稿
Identifierhttp://ir.ipe.ac.cn/handle/122111/5005
Collection研究所(批量导入)
AffiliationChinese Acad Sci, Inst Proc Engn, State Key Lab Biochem Engn, Beijing 100080, Peoples R China
Recommended Citation
GB/T 7714
Li, WJ,Su, ZG. Quantitatively investigating monomethoxypolyethylene glycol modification of protein by capillary electrophoresis[J]. JOURNAL OF BIOCHEMICAL AND BIOPHYSICAL METHODS,2004,59(1):65-74.
APA Li, WJ,&Su, ZG.(2004).Quantitatively investigating monomethoxypolyethylene glycol modification of protein by capillary electrophoresis.JOURNAL OF BIOCHEMICAL AND BIOPHYSICAL METHODS,59(1),65-74.
MLA Li, WJ,et al."Quantitatively investigating monomethoxypolyethylene glycol modification of protein by capillary electrophoresis".JOURNAL OF BIOCHEMICAL AND BIOPHYSICAL METHODS 59.1(2004):65-74.
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