Preparation and Characterization of a Chloroperoxidase-like Catalytic Antibody
The small molecule, meso-tetra(α,α,α,α-o-phenylacetamidophenyl) porphyrin (Mr1147.0) was used as complete antigen to elicit MAb through the immunization and cell fusion techniques. The MAb 1F2 obtained was demonstrated to be very pure by MALDI/TOFMS. The subtype of MAb 1F2 is IgG2a, which has a rela...
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| Format: | Online |
| Language: | English |
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Molecular Diversity Preservation International (MDPI)
2007
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| Online Access: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3692307/ |
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pubmed-36923072013-06-26 Preparation and Characterization of a Chloroperoxidase-like Catalytic Antibody Wang, Fengyang Huang, Xueying Du, Li Li, Weiguo He, Hongxuan Qi, Chao Full Research Paper The small molecule, meso-tetra(α,α,α,α-o-phenylacetamidophenyl) porphyrin (Mr1147.0) was used as complete antigen to elicit MAb through the immunization and cell fusion techniques. The MAb 1F2 obtained was demonstrated to be very pure by MALDI/TOFMS. The subtype of MAb 1F2 is IgG2a, which has a relative molecular weight of 156,678.8 Da.No significant change in the intensity of absorption peaks in UV and CD spectra was observed over a pH range between 6 and 12. The high stability of the abzyme and the tight binding between Fe porphyrin and antibody were also demonstrated. Vmax, Km, κcat, κcat/Km for abzyme are 5.18 × 10−8 Ms−1, 1.50 × 10−8 M, 0.518 s−1, 3.45 × 107 M−1s−1, respectively. The data obtained indicate that catalytic antibody has high catalytic activity. The chloroperoxidase activity of MAb 1F2-Fe porphyrin complex is stable from 10 °C to 60 °C. Molecular Diversity Preservation International (MDPI) 2007-05-29 /pmc/articles/PMC3692307/ Text en © 2007 by MDPI Reproduction is permitted for noncommercial purposes. |
| repository_type |
Open Access Journal |
| institution_category |
Foreign Institution |
| institution |
US National Center for Biotechnology Information |
| building |
NCBI PubMed |
| collection |
Online Access |
| language |
English |
| format |
Online |
| author |
Wang, Fengyang Huang, Xueying Du, Li Li, Weiguo He, Hongxuan Qi, Chao |
| spellingShingle |
Wang, Fengyang Huang, Xueying Du, Li Li, Weiguo He, Hongxuan Qi, Chao Preparation and Characterization of a Chloroperoxidase-like Catalytic Antibody |
| author_facet |
Wang, Fengyang Huang, Xueying Du, Li Li, Weiguo He, Hongxuan Qi, Chao |
| author_sort |
Wang, Fengyang |
| title |
Preparation and Characterization of a Chloroperoxidase-like Catalytic Antibody |
| title_short |
Preparation and Characterization of a Chloroperoxidase-like Catalytic Antibody |
| title_full |
Preparation and Characterization of a Chloroperoxidase-like Catalytic Antibody |
| title_fullStr |
Preparation and Characterization of a Chloroperoxidase-like Catalytic Antibody |
| title_full_unstemmed |
Preparation and Characterization of a Chloroperoxidase-like Catalytic Antibody |
| title_sort |
preparation and characterization of a chloroperoxidase-like catalytic antibody |
| description |
The small molecule, meso-tetra(α,α,α,α-o-phenylacetamidophenyl) porphyrin (Mr1147.0) was used as complete antigen to elicit MAb through the immunization and cell fusion techniques. The MAb 1F2 obtained was demonstrated to be very pure by MALDI/TOFMS. The subtype of MAb 1F2 is IgG2a, which has a relative molecular weight of 156,678.8 Da.No significant change in the intensity of absorption peaks in UV and CD spectra was observed over a pH range between 6 and 12. The high stability of the abzyme and the tight binding between Fe porphyrin and antibody were also demonstrated. Vmax, Km, κcat, κcat/Km for abzyme are 5.18 × 10−8 Ms−1, 1.50 × 10−8 M, 0.518 s−1, 3.45 × 107 M−1s−1, respectively. The data obtained indicate that catalytic antibody has high catalytic activity. The chloroperoxidase activity of MAb 1F2-Fe porphyrin complex is stable from 10 °C to 60 °C. |
| publisher |
Molecular Diversity Preservation International (MDPI) |
| publishDate |
2007 |
| url |
https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3692307/ |
| _version_ |
1611989373798055936 |