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Protein structure of the venom in nine species of snake: from bio-compounds to possible healing agents

Due to its various structures in bio-compounds, snake venom is the indisputable result of evolutionary stages of molecules with an increasingly complex structure, high specificity, and of great importance for medicine because of their potential. The present study proposed an underpinning examination...

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Autores principales: Cristina, R.T., Kocsis, R., Tulcan, C., Alexa, E., Boldura, O.M., Hulea, C.I., Dumitrescu, E., Radulov, I., Muselin, F.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Associação Brasileira de Divulgação Científica 2020
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6967130/
https://www.ncbi.nlm.nih.gov/pubmed/31939598
http://dx.doi.org/10.1590/1414-431X20199001
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author Cristina, R.T.
Kocsis, R.
Tulcan, C.
Alexa, E.
Boldura, O.M.
Hulea, C.I.
Dumitrescu, E.
Radulov, I.
Muselin, F.
author_facet Cristina, R.T.
Kocsis, R.
Tulcan, C.
Alexa, E.
Boldura, O.M.
Hulea, C.I.
Dumitrescu, E.
Radulov, I.
Muselin, F.
author_sort Cristina, R.T.
collection PubMed
description Due to its various structures in bio-compounds, snake venom is the indisputable result of evolutionary stages of molecules with an increasingly complex structure, high specificity, and of great importance for medicine because of their potential. The present study proposed an underpinning examination of venom composition from nine species of venomous snakes using a useful and replicable methodology. The objective was the extension of the evaluation of protein fractions in the field up to 230 kDa to permit possible identification of some fractions that are insufficiently studied. The gel capillary electrophoresis method on the chip was performed using an Agilent 2100 bioassay with the 80 and 230-LabChip Protein kits. Interpretation of electrophoresis was performed using the Protein 2100 expert (Agilent) test software as follows: a) Protein 80 (peak size scale): 1.60, 3.5, 6.50, 15.00, 28.00, 46.00, 63.00, 95.00 kDa; b) Protein 230 (peak size scale): 4.50, 7.00, 15.00, 28.00, 46.00, 63.00, 95.00, 150.00, 240.00 kDa. The screening revealed the presence of compounds with a molecular weight greater than 80 kDa, in the case of Vipera aspis and Vipera xantina palestinae. For V. aspis, a 125 kDa molecular weight pro-coagulant protein was identified, known as being involved in the reduction of plasma clotting time without any direct activity in the fibrinogen coagulation process. The samples examined on the Protein 230-LabChip electrophoresis chip can be considered as a novelty with possible uses in medicine, requiring further approaches by advanced proteomics techniques to confirm the intimate structural features and biological properties of snake venoms.
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spelling pubmed-69671302020-01-30 Protein structure of the venom in nine species of snake: from bio-compounds to possible healing agents Cristina, R.T. Kocsis, R. Tulcan, C. Alexa, E. Boldura, O.M. Hulea, C.I. Dumitrescu, E. Radulov, I. Muselin, F. Braz J Med Biol Res Research Article Due to its various structures in bio-compounds, snake venom is the indisputable result of evolutionary stages of molecules with an increasingly complex structure, high specificity, and of great importance for medicine because of their potential. The present study proposed an underpinning examination of venom composition from nine species of venomous snakes using a useful and replicable methodology. The objective was the extension of the evaluation of protein fractions in the field up to 230 kDa to permit possible identification of some fractions that are insufficiently studied. The gel capillary electrophoresis method on the chip was performed using an Agilent 2100 bioassay with the 80 and 230-LabChip Protein kits. Interpretation of electrophoresis was performed using the Protein 2100 expert (Agilent) test software as follows: a) Protein 80 (peak size scale): 1.60, 3.5, 6.50, 15.00, 28.00, 46.00, 63.00, 95.00 kDa; b) Protein 230 (peak size scale): 4.50, 7.00, 15.00, 28.00, 46.00, 63.00, 95.00, 150.00, 240.00 kDa. The screening revealed the presence of compounds with a molecular weight greater than 80 kDa, in the case of Vipera aspis and Vipera xantina palestinae. For V. aspis, a 125 kDa molecular weight pro-coagulant protein was identified, known as being involved in the reduction of plasma clotting time without any direct activity in the fibrinogen coagulation process. The samples examined on the Protein 230-LabChip electrophoresis chip can be considered as a novelty with possible uses in medicine, requiring further approaches by advanced proteomics techniques to confirm the intimate structural features and biological properties of snake venoms. Associação Brasileira de Divulgação Científica 2020-01-13 /pmc/articles/PMC6967130/ /pubmed/31939598 http://dx.doi.org/10.1590/1414-431X20199001 Text en https://creativecommons.org/licenses/by/4.0/ This is an Open Access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Research Article
Cristina, R.T.
Kocsis, R.
Tulcan, C.
Alexa, E.
Boldura, O.M.
Hulea, C.I.
Dumitrescu, E.
Radulov, I.
Muselin, F.
Protein structure of the venom in nine species of snake: from bio-compounds to possible healing agents
title Protein structure of the venom in nine species of snake: from bio-compounds to possible healing agents
title_full Protein structure of the venom in nine species of snake: from bio-compounds to possible healing agents
title_fullStr Protein structure of the venom in nine species of snake: from bio-compounds to possible healing agents
title_full_unstemmed Protein structure of the venom in nine species of snake: from bio-compounds to possible healing agents
title_short Protein structure of the venom in nine species of snake: from bio-compounds to possible healing agents
title_sort protein structure of the venom in nine species of snake: from bio-compounds to possible healing agents
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6967130/
https://www.ncbi.nlm.nih.gov/pubmed/31939598
http://dx.doi.org/10.1590/1414-431X20199001
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