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Recombinant Protein L: Production, Purification and Characterization of a Universal Binding Ligand
被引:5
作者:
Kittler, Stefan
[1
,2
]
Ebner, Julian
[1
,2
]
Besleaga, Mihail
[1
]
Larsbrink, Johan
[3
]
Darnhofer, Barbara
[4
]
Birner-Gruenberger, Ruth
[4
,5
]
Schobesberger, Silvia
[6
]
Akhgar, Christopher K.
[7
]
Schwaighofer, Andreas
[7
]
Lendl, Bernhard
[7
]
Spadiut, Oliver
[1
]
机构:
[1] TU Wien, Inst Chem Environm & Biosci Engn, Res Div Integrated Bioproc Dev, Gumpendorfer Str 1a, A-1060 Vienna, Austria
[2] Alfred Gruber GmbH, Nordstr 6, A-5301 Eugendorf, Austria
[3] Chalmers Univ Technol, Wallenberg Wood Sci Ctr, Dept Biol & Biol Engn, Div Ind Biotechnol, Gothenburg, Sweden
[4] Med Univ Graz, Diagnost & Res Inst Pathol, Res Div Funct Prote & Metab Pathways, Stiftingtalstr 24, A-8010 Graz, Austria
[5] TU Wien, Inst Chem Technol & Analyt, Res Div Bioanalyt, Getreidemarkt 9-164, A-1060 Vienna, Austria
[6] TU Wien, Inst Appl Synthet Chem, Res Div Organ & Biol Chem, Getreidemarkt 9-163, A-1060 Vienna, Austria
[7] TU Wien, Inst Chem Technol & Analyt, Res Div Environm Analyt Proc Analyt & Sensors, Getreidemarkt 9-164, A-1060 Vienna, Austria
关键词:
Protein L;
E;
coli;
Recombinant production;
Bioreactor;
Affinity ligand;
HISTIDINE-TAGGED PROTEINS;
PEPTOSTREPTOCOCCUS-MAGNUS;
IMMOBILIZATION;
AFFINITY;
GLUTARALDEHYDE;
EXPRESSION;
ANTIBODIES;
DOMAINS;
D O I:
10.1016/j.jbiotec.2022.10.002
中图分类号:
Q81 [生物工程学(生物技术)];
Q93 [微生物学];
学科分类号:
071005 ;
0836 ;
090102 ;
100705 ;
摘要:
Protein L (PpL) is a universal binding ligand that can be used for the detection and purification of antibodies and antibody fragments. Due to the unique interaction with immunoglobulin light chains, it differs from other affinity ligands, like protein A or G. However, due to its current higher market price, PpL is still scarce in applications. In this study, we investigated the recombinant production and purification of PpL and characterized the product in detail. We present a comprehensive roadmap for the production of the versatile protein PpL in E. coli.
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页码:108 / 115
页数:8
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