Single-chain Fv fragment lacks carrier specificity of the native antibody
Publication in refereed journal


香港中文大学研究人员 ( 现职)

崔耀隆教授 (化学病理学系)

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数位物件识别号 (DOI) http://dx.doi.org/10.1016/S0161-5890(02)00056-1

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Web of Sciencehttp://aims.cuhk.edu.hk/converis/portal/Publication/5WOS source URL

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摘要A single-chain antibody fragment (scFv) was constructed from a hybridoma antibody that binds to phosphorylcholine (PC) only when this hapten is presented in the form of the immunizing antigen (derived from Trichinella) but not when it is presented on other carriers (as found, for example, in pneumococcal capsules). The scFv derivative was found to lack this carrier specificity as it bound indiscriminately, but specifically, to the various PC-associated antigens, and exhibits a two-fold lower affinity (3.http://aims.cuhk.edu.hk/converis/portal/Publication/5 x 10(http://aims.cuhk.edu.hk/converis/portal/Publication/5) M-1) for nitrophenyl-PC than the native antibody. The findings suggest that the scFv combining site is different in fine structure from that of the native antibody. (C) 2002 Elsevier Science Ltd. All rights reserved.

着者Poon KM, Tam FCH, Chui YL, Lim PL
期刊名称MOLECULAR IMMUNOLOGY
出版年份2002
月份9
日期1
卷号39
期次1-2
出版社PERGAMON-ELSEVIER SCIENCE LTD
页次19 - 24
国际标準期刊号0161-http://aims.cuhk.edu.hk/converis/portal/Publication/5890
语言英式英语

关键词affinity; phage-display; phosphorylcholine; Trichinella
Web of Science 学科类别Biochemistry & Molecular Biology; BIOCHEMISTRY & MOLECULAR BIOLOGY; Immunology; IMMUNOLOGY