Title of article :
Isolation of novel catalytic antibody clones from combinatorial library displayed on yeast-cell surface
Author/Authors :
Lin، نويسنده , , Ying and Shiraga، نويسنده , , Seizaburo and Tsumuraya، نويسنده , , Takeshi and Fujii، نويسنده , , Ikuo and Matsumoto، نويسنده , , Takeshi and Kondo، نويسنده , , Akihiko and Ueda، نويسنده , , Mitsuyoshi، نويسنده ,
Issue Information :
روزنامه با شماره پیاپی سال 2004
Pages :
5
From page :
247
To page :
251
Abstract :
A combinatorial library of the Fab fragment of a catalytic antibody able to hydrolyze a non-bioactive chloramphenicol monoester derivative to produce chloramphenicol was constructed on yeast-cell surface. Interesting clones were selected using fluorescence-activated cell sorting (FACS). When binding affinity to a transition-state analog was detected, evolution of the catalytic antibody was carried out in vitro on yeast-cell surface. A number of variants with enhanced catalytic activity and binding affinity were obtained. The results showed that the improvement of catalytic antibody, which can be performed easily on yeast-cell surface using the cell-surface engineering system, is a good example of the application of protein library construction.
Keywords :
combinatorial library , Catalytic antibody , Yeast-cell surface engineering , Molecular display , molecular evolution
Journal title :
Journal of Molecular Catalysis B Enzymatic
Serial Year :
2004
Journal title :
Journal of Molecular Catalysis B Enzymatic
Record number :
1710139
Link To Document :
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