Beneficial properties of single-domain antibody fragments for application in immunoaffinity purification and immuno-perfasion chromatography

被引:58
作者
Verheesen, P
ten Haaft, MR
Lindner, N
Verrips, CT
de Haard, JJW
机构
[1] Univ Utrecht, Dept Mol & Cellular Biol, NL-3500 TB Utrecht, Netherlands
[2] Biotechnol Applicat Ctr BV, NL-1400 CA Bussum, Netherlands
[3] Unilever Res Labs, Sharnbrook MK44 1LQ, Beds, England
[4] Unilever Res, Dept Microbial Biotechnol, Vlaardingen Lab, NL-3133 AT Vlaardingen, Netherlands
来源
BIOCHIMICA ET BIOPHYSICA ACTA-GENERAL SUBJECTS | 2003年 / 1624卷 / 1-3期
关键词
single-domain antibody fragment; phage display; immunoaffinity chromatography; ice structuring protein; protein purification;
D O I
10.1016/j.bbagen.2003.09.006
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
We explored the possibility to apply single-domain antibodies from Camelidae for immunoaffinity purification of the ice structuring protein (ISP) from Lolium perenne, which modifies ice crystal growth and therefore has potential application in medicine, biotechnology, agriculture and (frozen) foods. Using phage display together with an appropriate selection method, a group of candidate fragments was isolated from a llama-derived immune library. Affinity chromatography using a purposely selected antibody coupled to a matrix yielded a completely pure and functional ISP. Due to the extreme refolding capabilities and physical stability of single-domain antibodies, the affinity matrix could be regenerated more than 2000 times without loss of capacity, while the fragment's monomeric nature permitted an efficient elution of antigen. The results of this study show that highly pure proteins can be recovered from biological material in a single-step process. (C) 2003 Elsevier B.V. All rights reserved.
引用
收藏
页码:21 / 28
页数:8
相关论文
共 34 条
[1]   FLOW-THROUGH PARTICLES FOR THE HIGH-PERFORMANCE LIQUID-CHROMATOGRAPHIC SEPARATION OF BIOMOLECULES - PERFUSION CHROMATOGRAPHY [J].
AFEYAN, NB ;
GORDON, NF ;
MAZSAROFF, I ;
VARADY, L ;
FULTON, SP ;
YANG, YB ;
REGNIER, FE .
JOURNAL OF CHROMATOGRAPHY, 1990, 519 (01) :1-29
[2]   A minimal peptide substrate in biotin holoenzyme synthetase-catalyzed biotinylation [J].
Beckett, D ;
Kovaleva, E ;
Schatz, PJ .
PROTEIN SCIENCE, 1999, 8 (04) :921-929
[3]   Advances in gentle immunoaffinity chromatography [J].
Burgess, RR ;
Thompson, NE .
CURRENT OPINION IN BIOTECHNOLOGY, 2002, 13 (04) :304-308
[4]  
Chao HM, 1996, J EXP BIOL, V199, P2071
[5]  
Clarke CJ, 2002, CRYOLETTERS, V23, P89
[6]   A simple method for midkine purification by affinity chromatography with a heavy chain variable domain (VH) fragment of antibody [J].
Dansithong, W ;
Paul, S ;
Kojima, Y ;
Kamiya, K ;
Shinozawa, T .
JOURNAL OF BIOCHEMICAL AND BIOPHYSICAL METHODS, 2001, 48 (01) :77-84
[7]   Selection of recombinant, library-derived antibody fragments against p24 for human immunodeficiency virus type 1 diagnostics [J].
de Haard, HJW ;
Kazemier, B ;
Koolen, MJM ;
Nijholt, LJ ;
Meloen, RH ;
van Gemen, B ;
Hoogenboom, HR ;
Arends, JW .
CLINICAL AND DIAGNOSTIC LABORATORY IMMUNOLOGY, 1998, 5 (05) :636-644
[8]  
DITZEL HJ, 1995, J IMMUNOL, V154, P893
[9]  
Fletcher GL, 1999, CHEMTECH, V29, P17
[10]   Isolation of antigen specific Llama VHH antibody fragments and their high level secretion by Saccharomyces cerevisiae [J].
Frenken, LGJ ;
van der Linden, RHJ ;
Hermans, PWJJ ;
Bos, JW ;
Ruuls, RC ;
de Geus, B ;
Verrips, CT .
JOURNAL OF BIOTECHNOLOGY, 2000, 78 (01) :11-21