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Characterization, antimicrobial and antitumor activity of superoxide dismutase extracted from Egyptian honeybee venom (Apis mellifera lamarckii)

BACKGROUND: Superoxide dismutase is an important antioxidative stress enzyme which is found in honeybee venom and has a wide pharmaceutical and medical applications. RESULTS: We reported the purification and characterization of venom SOD from Egyptian honeybee Apis mellifera lamarckii and termed BVS...

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Autores principales: Abdel-Monsef, Mohamed M., Darwish, Doaa A., Zidan, Hind A., Hamed, Ahmed A., Ibrahim, Mahmoud A.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Springer Berlin Heidelberg 2023
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9941395/
https://www.ncbi.nlm.nih.gov/pubmed/36807019
http://dx.doi.org/10.1186/s43141-023-00470-4
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author Abdel-Monsef, Mohamed M.
Darwish, Doaa A.
Zidan, Hind A.
Hamed, Ahmed A.
Ibrahim, Mahmoud A.
author_facet Abdel-Monsef, Mohamed M.
Darwish, Doaa A.
Zidan, Hind A.
Hamed, Ahmed A.
Ibrahim, Mahmoud A.
author_sort Abdel-Monsef, Mohamed M.
collection PubMed
description BACKGROUND: Superoxide dismutase is an important antioxidative stress enzyme which is found in honeybee venom and has a wide pharmaceutical and medical applications. RESULTS: We reported the purification and characterization of venom SOD from Egyptian honeybee Apis mellifera lamarckii and termed BVSOD. It was purified to homogeneity from the Egyptian honeybee venom. The purification procedures included crude extraction, DEAE-cellulose anion exchange column chromatography, and Sephacryl S-300 gel filtration column chromatography. The purified BVSOD is found to be homogeneous as investigated by native PAGE. It exhibited homodimeric structure with a molecular weight of native form of 32 kDa and subunits of 16.0 kDa. It displayed the maximum activity at pH 7.4. CuCl(2), ZnCl(2), and MgCl(2) and elevated the activity of BVSOD, while CoCl(2), FeCl(2), and NiCl(2) inhibited BVSOD activity. Potassium cyanide and hydrogen peroxide were most potent inhibitors for BVSOD activity suggesting that it is a Cu/Zn-SOD type. CONCLUSIONS: The purified BVSOD is found to have antimicrobial and antitumor activities which can be used for various medical and clinical applications.
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spelling pubmed-99413952023-02-22 Characterization, antimicrobial and antitumor activity of superoxide dismutase extracted from Egyptian honeybee venom (Apis mellifera lamarckii) Abdel-Monsef, Mohamed M. Darwish, Doaa A. Zidan, Hind A. Hamed, Ahmed A. Ibrahim, Mahmoud A. J Genet Eng Biotechnol Research BACKGROUND: Superoxide dismutase is an important antioxidative stress enzyme which is found in honeybee venom and has a wide pharmaceutical and medical applications. RESULTS: We reported the purification and characterization of venom SOD from Egyptian honeybee Apis mellifera lamarckii and termed BVSOD. It was purified to homogeneity from the Egyptian honeybee venom. The purification procedures included crude extraction, DEAE-cellulose anion exchange column chromatography, and Sephacryl S-300 gel filtration column chromatography. The purified BVSOD is found to be homogeneous as investigated by native PAGE. It exhibited homodimeric structure with a molecular weight of native form of 32 kDa and subunits of 16.0 kDa. It displayed the maximum activity at pH 7.4. CuCl(2), ZnCl(2), and MgCl(2) and elevated the activity of BVSOD, while CoCl(2), FeCl(2), and NiCl(2) inhibited BVSOD activity. Potassium cyanide and hydrogen peroxide were most potent inhibitors for BVSOD activity suggesting that it is a Cu/Zn-SOD type. CONCLUSIONS: The purified BVSOD is found to have antimicrobial and antitumor activities which can be used for various medical and clinical applications. Springer Berlin Heidelberg 2023-02-20 /pmc/articles/PMC9941395/ /pubmed/36807019 http://dx.doi.org/10.1186/s43141-023-00470-4 Text en © The Author(s) 2023 https://creativecommons.org/licenses/by/4.0/Open AccessThis article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/ (https://creativecommons.org/licenses/by/4.0/) .
spellingShingle Research
Abdel-Monsef, Mohamed M.
Darwish, Doaa A.
Zidan, Hind A.
Hamed, Ahmed A.
Ibrahim, Mahmoud A.
Characterization, antimicrobial and antitumor activity of superoxide dismutase extracted from Egyptian honeybee venom (Apis mellifera lamarckii)
title Characterization, antimicrobial and antitumor activity of superoxide dismutase extracted from Egyptian honeybee venom (Apis mellifera lamarckii)
title_full Characterization, antimicrobial and antitumor activity of superoxide dismutase extracted from Egyptian honeybee venom (Apis mellifera lamarckii)
title_fullStr Characterization, antimicrobial and antitumor activity of superoxide dismutase extracted from Egyptian honeybee venom (Apis mellifera lamarckii)
title_full_unstemmed Characterization, antimicrobial and antitumor activity of superoxide dismutase extracted from Egyptian honeybee venom (Apis mellifera lamarckii)
title_short Characterization, antimicrobial and antitumor activity of superoxide dismutase extracted from Egyptian honeybee venom (Apis mellifera lamarckii)
title_sort characterization, antimicrobial and antitumor activity of superoxide dismutase extracted from egyptian honeybee venom (apis mellifera lamarckii)
topic Research
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9941395/
https://www.ncbi.nlm.nih.gov/pubmed/36807019
http://dx.doi.org/10.1186/s43141-023-00470-4
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