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Obtaining Highly Active Catalytic Antibodies Capable of Enzymatically Cleaving Antigens
A catalytic antibody has multiple functions compared with a monoclonal antibody because it possesses unique features to digest antigens enzymatically. Therefore, many catalytic antibodies, including their subunits, have been produced since 1989. The catalytic activities often depend on the preparati...
Autores principales: | , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2022
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9697424/ https://www.ncbi.nlm.nih.gov/pubmed/36430828 http://dx.doi.org/10.3390/ijms232214351 |
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author | Nonaka, Tamami Taguchi, Hiroaki Uda, Taizo Hifumi, Emi |
author_facet | Nonaka, Tamami Taguchi, Hiroaki Uda, Taizo Hifumi, Emi |
author_sort | Nonaka, Tamami |
collection | PubMed |
description | A catalytic antibody has multiple functions compared with a monoclonal antibody because it possesses unique features to digest antigens enzymatically. Therefore, many catalytic antibodies, including their subunits, have been produced since 1989. The catalytic activities often depend on the preparation methods and conditions. In order to elicit the high catalytic activity of the antibodies, the most preferable methods and conditions, which can be generally applicable, must be explored. Based on this view, systematic experiments using two catalytic antibody light chains, #7TR and H34, were performed by varying the purification methods, pH, and chemical reagents. The experimental results obtained by peptidase activity tests and kinetic analysis, revealed that the light chain’s high catalytic activity was observed when it was prepared under a basic condition. These data imply that a small structural modulation of the catalytic antibody occurs during the purification process to increase the catalytic activity while the antigen recognition ability is kept constant. The presence of NaCl enhanced the catalytic activity. When the catalytic light chain was prepared with these preferable conditions, #7TR and H34 hugely enhanced the degradation ability of Amyloid-beta and PD-1 peptide, respectively. |
format | Online Article Text |
id | pubmed-9697424 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-96974242022-11-26 Obtaining Highly Active Catalytic Antibodies Capable of Enzymatically Cleaving Antigens Nonaka, Tamami Taguchi, Hiroaki Uda, Taizo Hifumi, Emi Int J Mol Sci Article A catalytic antibody has multiple functions compared with a monoclonal antibody because it possesses unique features to digest antigens enzymatically. Therefore, many catalytic antibodies, including their subunits, have been produced since 1989. The catalytic activities often depend on the preparation methods and conditions. In order to elicit the high catalytic activity of the antibodies, the most preferable methods and conditions, which can be generally applicable, must be explored. Based on this view, systematic experiments using two catalytic antibody light chains, #7TR and H34, were performed by varying the purification methods, pH, and chemical reagents. The experimental results obtained by peptidase activity tests and kinetic analysis, revealed that the light chain’s high catalytic activity was observed when it was prepared under a basic condition. These data imply that a small structural modulation of the catalytic antibody occurs during the purification process to increase the catalytic activity while the antigen recognition ability is kept constant. The presence of NaCl enhanced the catalytic activity. When the catalytic light chain was prepared with these preferable conditions, #7TR and H34 hugely enhanced the degradation ability of Amyloid-beta and PD-1 peptide, respectively. MDPI 2022-11-18 /pmc/articles/PMC9697424/ /pubmed/36430828 http://dx.doi.org/10.3390/ijms232214351 Text en © 2022 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Article Nonaka, Tamami Taguchi, Hiroaki Uda, Taizo Hifumi, Emi Obtaining Highly Active Catalytic Antibodies Capable of Enzymatically Cleaving Antigens |
title | Obtaining Highly Active Catalytic Antibodies Capable of Enzymatically Cleaving Antigens |
title_full | Obtaining Highly Active Catalytic Antibodies Capable of Enzymatically Cleaving Antigens |
title_fullStr | Obtaining Highly Active Catalytic Antibodies Capable of Enzymatically Cleaving Antigens |
title_full_unstemmed | Obtaining Highly Active Catalytic Antibodies Capable of Enzymatically Cleaving Antigens |
title_short | Obtaining Highly Active Catalytic Antibodies Capable of Enzymatically Cleaving Antigens |
title_sort | obtaining highly active catalytic antibodies capable of enzymatically cleaving antigens |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9697424/ https://www.ncbi.nlm.nih.gov/pubmed/36430828 http://dx.doi.org/10.3390/ijms232214351 |
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