Preparation and Characterization of a Chloroperoxidase-like Catalytic Antibody

International Journal of Molecular Sciences

Fengyang Wang¹  Xueying Huang²  Li Du¹  Weiguo Li²  Hongxuan He³ 

[1] College of Life Science and Agriculture, Key Laboratory of Tropic Biological Resources of Ministry of Education, Hainan University, Haikou 570228, P.R. China; E-mail:;College of Chemistry, Huazhong Normal University, Wuhan 430079, P. R. China; E-mail:;Research Center for Wildlife Animal Diseases, Key Laboratory of Animal Ecology and Conservation Biology, Institute of Zoology, Chinese Academy of Sciences, Beijing 100080, P. R. China; E-mail:

关键词: meso- Tetra porphyrin;    MAb;    Complete antigen;    Chloroperoxidase;    Abzyme;   

DOI  :  10.3390/i8050445

来源: mdpi

【 摘 要 】

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. V_max, K_m, κcat, κcat/K_m 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.

【 授权许可】

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