Document Detail


Construction of affinity changeable antibody in response to Ca(2+).
MedLine Citation:
PMID:  22350334     Owner:  NLM     Status:  Publisher    
Abstract/OtherAbstract:
Immunoaffinity chromatography is a powerful method for purification of proteins because of the high selectivity and avidity of antibodies. Due to the strength of antigen-antibody binding, however, elution of proteins bound to antibodies that are covalently immobilized on the column is performed by temporary denaturation of the antibody. Therefore, the development of milder elution conditions could improve the recovery of the antibodies and prolong the life of the immunoaffinity column. We describe the design and construction of an antibody that changes its affinity in response to external stimuli. The heavy chain and light chain of a single chain Fv of the D1.3 antibody against hen egg-white lysozyme (HEL) were fused at the N- and C-termini, respectively, of the calmodulin-M13 fusion protein. The affinity of this fusion protein for HEL could be modulated by changing the Ca(2+) concentration.
Authors:
Eiry Kobatake; Chihiro Kosaku; Satoshi Hanzawa; Masayasu Mie
Related Documents :
23971754 - B-cell-targeted therapies in systemic lupus erythematosus and anca-associated vasculiti...
15135864 - Characterisation of theileria parva isolates from kiambu district, kenya.
2414204 - The characterization of two monoclonal anti-keratin antibodies and their use in the stu...
1541564 - Isolation and characterization of a recombinant antigen of pneumocystis carinii.
9203024 - The role of heat shock protein, microbial and autoimmune agents in the aetiology of beh...
6270954 - A "reverse" solid-phase radio-immuno-assay for igm-antibodies to hepatitis a virus.
Publication Detail:
Type:  JOURNAL ARTICLE     Date:  2012-2-21
Journal Detail:
Title:  Biotechnology letters     Volume:  -     ISSN:  1573-6776     ISO Abbreviation:  -     Publication Date:  2012 Feb 
Date Detail:
Created Date:  2012-2-21     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  8008051     Medline TA:  Biotechnol Lett     Country:  -    
Other Details:
Languages:  ENG     Pagination:  -     Citation Subset:  -    
Affiliation:
Department of Biological Information, Graduate School of Bioscience and Biotechnology, Tokyo Institute of Technology, 4259 Nagatsuta, Midori-ku, Yokohama, 226-8501, Japan, ekobatak@bio.titech.ac.jp.
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
Descriptor/Qualifier:

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


Previous Document:  Cloning, expression, characterization and application of atcA, atcB and atcC from Pseudomonas sp. fo...
Next Document:  Improving the acidic stability of a methyl parathion hydrolase by changing basic residues to acidic ...