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Proteolytic activity of Elapid and Viperid Snake venoms and its implication to digestion
Testing whether venoms may aid in digestion of the prey, eleven snake venoms were compared for the presence of proteases and endopeptidases that function in alkaline pH conditions. In vitro experiments examined the relative protease and endopeptidase activity of the venoms, which involved combining...
Autores principales: | , , , , |
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Formato: | Texto |
Lenguaje: | English |
Publicado: |
Library Publishing Media
2010
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3086185/ https://www.ncbi.nlm.nih.gov/pubmed/21544178 |
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author | Bottrall, Joshua L Madaras, Frank Biven, Christopher D Venning, Michael G Mirtschin, Peter J |
author_facet | Bottrall, Joshua L Madaras, Frank Biven, Christopher D Venning, Michael G Mirtschin, Peter J |
author_sort | Bottrall, Joshua L |
collection | PubMed |
description | Testing whether venoms may aid in digestion of the prey, eleven snake venoms were compared for the presence of proteases and endopeptidases that function in alkaline pH conditions. In vitro experiments examined the relative protease and endopeptidase activity of the venoms, which involved combining bovine muscle and snake venom in a buffered solution, encased within dialysis tubing. This mixture was then incubated at room temperature (∼20°C) for 24hr, with constant shaking. Bicinchoninic acid (BCA) assay and ninhydrin assay were used to determine peptide and amino acid concentrations. Histological and immunohistochemical investigations using N. kaouthia venom confirmed in vitro findings. Results show that B. arietans venom generated the highest amount of protein/peptides and amino acids in the dialysates, while O. scutellatus, N. ater niger and P. textilis venom did not show any significant protein degradation under alkaline conditions. Histological examination revealed varying degrees of muscle cell damage for each of the venom investigated, and the immunohistochemical study on N. kaouthia venom showed that the venom penetrated the muscle tissue to a significant degree. In vitro assays and histological results indicate that particular venoms may possess the ability to enhance digestion of bovine muscle tissue. |
format | Text |
id | pubmed-3086185 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2010 |
publisher | Library Publishing Media |
record_format | MEDLINE/PubMed |
spelling | pubmed-30861852011-05-04 Proteolytic activity of Elapid and Viperid Snake venoms and its implication to digestion Bottrall, Joshua L Madaras, Frank Biven, Christopher D Venning, Michael G Mirtschin, Peter J J Venom Res Research Article Testing whether venoms may aid in digestion of the prey, eleven snake venoms were compared for the presence of proteases and endopeptidases that function in alkaline pH conditions. In vitro experiments examined the relative protease and endopeptidase activity of the venoms, which involved combining bovine muscle and snake venom in a buffered solution, encased within dialysis tubing. This mixture was then incubated at room temperature (∼20°C) for 24hr, with constant shaking. Bicinchoninic acid (BCA) assay and ninhydrin assay were used to determine peptide and amino acid concentrations. Histological and immunohistochemical investigations using N. kaouthia venom confirmed in vitro findings. Results show that B. arietans venom generated the highest amount of protein/peptides and amino acids in the dialysates, while O. scutellatus, N. ater niger and P. textilis venom did not show any significant protein degradation under alkaline conditions. Histological examination revealed varying degrees of muscle cell damage for each of the venom investigated, and the immunohistochemical study on N. kaouthia venom showed that the venom penetrated the muscle tissue to a significant degree. In vitro assays and histological results indicate that particular venoms may possess the ability to enhance digestion of bovine muscle tissue. Library Publishing Media 2010-09-30 /pmc/articles/PMC3086185/ /pubmed/21544178 Text en ©The Authors http://creativecommons.org/licenses/by-nc/2.0/uk/ This is an open access article, published under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.0/uk/). This license permits non-commercial use, distribution and reproduction of the article, provided the original work is appropriately acknowledged with correct citation details. |
spellingShingle | Research Article Bottrall, Joshua L Madaras, Frank Biven, Christopher D Venning, Michael G Mirtschin, Peter J Proteolytic activity of Elapid and Viperid Snake venoms and its implication to digestion |
title | Proteolytic activity of Elapid and Viperid Snake venoms and its implication to digestion |
title_full | Proteolytic activity of Elapid and Viperid Snake venoms and its implication to digestion |
title_fullStr | Proteolytic activity of Elapid and Viperid Snake venoms and its implication to digestion |
title_full_unstemmed | Proteolytic activity of Elapid and Viperid Snake venoms and its implication to digestion |
title_short | Proteolytic activity of Elapid and Viperid Snake venoms and its implication to digestion |
title_sort | proteolytic activity of elapid and viperid snake venoms and its implication to digestion |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3086185/ https://www.ncbi.nlm.nih.gov/pubmed/21544178 |
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