Snake venoms are important sources of complex substances with a variety of pharmacological activities. Among them serine proteinases (SVSPs) have important effects on the hemostatic system influencing the hemodynamic of human or animal blood. Bothrops genus-snake venoms are rich in the thrombin-like enzyme, a type of SVSPs, with great interest to produce medicine. Therefore, the aim of this work was to describe a rapid, only two-step chromatographic-procedure developed to perform a faster purification of SVSPs from Bothrops alternatus and Bothrops moojeni venoms. As a result, two groups of serine proteinases respectively BaIII-4 - 8 and BmIII-2 - 5, were isolated and their molecular masses estimated by mass spectrometry and SDS-PAGE under denaturing conditions. The SVTLEs isolated from B. alternatus (BaIII-3 - 8) and B. moojeni (BmIII-2 - 5) fractions displayed apparent molecular mass around 30-40 kDa which closely relates to SVTLEs from other Bothrops species, as well their amino acid partial sequence triptych ions. Analysis of the alignment of the amino acid residue sequences of the N-terminal of the isolated proteins revealed a high level of identity with other SVTLEs. These enzymes coagulated plasma and showed fibrinogenolytic activity in blood. These SVTLEs isolated can be considered α-fibrinogenase mainly due to the fact that they hydrolyze the Aα chain fibrinogen. B. moojeni SVTLE showed greater activity than those from B. alternatus isolated. This new purification alternative approach developed was faster and more economical than the traditional process currently used. Faster purification and improved extraction yield can provide new insights into these enzymes including the use as a candidate molecule in the production of new drugs.
| Published in | American Journal of Biomedical and Life Sciences (Volume 9, Issue 4) |
| DOI | 10.11648/j.ajbls.20210904.15 |
| Page(s) | 209-218 |
| Creative Commons |
This is an Open Access article, distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution and reproduction in any medium or format, provided the original work is properly cited. |
| Copyright |
Copyright © The Author(s), 2024. Published by Science Publishing Group |
Bothrops alternatus, Bothrops moojeni, Serine Proteinases, Thrombin-like Enzyme, Fast Purification
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APA Style
Mauricio Aurelio Gomes Heleno, Edda Evnet Newball-Noriega, Salomón Huancahuire-Vega, Rui Seabra Ferreira Júnior, Benedito Barraviera. (2021). A Novel Fast and Efficient Approach to Purify the Thrombin-like Enzyme from Two Bothrops-genus Snake Venoms. American Journal of Biomedical and Life Sciences, 9(4), 209-218. https://doi.org/10.11648/j.ajbls.20210904.15
ACS Style
Mauricio Aurelio Gomes Heleno; Edda Evnet Newball-Noriega; Salomón Huancahuire-Vega; Rui Seabra Ferreira Júnior; Benedito Barraviera. A Novel Fast and Efficient Approach to Purify the Thrombin-like Enzyme from Two Bothrops-genus Snake Venoms. Am. J. Biomed. Life Sci. 2021, 9(4), 209-218. doi: 10.11648/j.ajbls.20210904.15
AMA Style
Mauricio Aurelio Gomes Heleno, Edda Evnet Newball-Noriega, Salomón Huancahuire-Vega, Rui Seabra Ferreira Júnior, Benedito Barraviera. A Novel Fast and Efficient Approach to Purify the Thrombin-like Enzyme from Two Bothrops-genus Snake Venoms. Am J Biomed Life Sci. 2021;9(4):209-218. doi: 10.11648/j.ajbls.20210904.15
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Download@article{10.11648/j.ajbls.20210904.15,
author = {Mauricio Aurelio Gomes Heleno and Edda Evnet Newball-Noriega and Salomón Huancahuire-Vega and Rui Seabra Ferreira Júnior and Benedito Barraviera},
title = {A Novel Fast and Efficient Approach to Purify the Thrombin-like Enzyme from Two Bothrops-genus Snake Venoms},
journal = {American Journal of Biomedical and Life Sciences},
volume = {9},
number = {4},
pages = {209-218},
doi = {10.11648/j.ajbls.20210904.15},
url = {https://doi.org/10.11648/j.ajbls.20210904.15},
eprint = {https://article.sciencepublishinggroup.com/pdf/10.11648.j.ajbls.20210904.15},
abstract = {Snake venoms are important sources of complex substances with a variety of pharmacological activities. Among them serine proteinases (SVSPs) have important effects on the hemostatic system influencing the hemodynamic of human or animal blood. Bothrops genus-snake venoms are rich in the thrombin-like enzyme, a type of SVSPs, with great interest to produce medicine. Therefore, the aim of this work was to describe a rapid, only two-step chromatographic-procedure developed to perform a faster purification of SVSPs from Bothrops alternatus and Bothrops moojeni venoms. As a result, two groups of serine proteinases respectively BaIII-4 - 8 and BmIII-2 - 5, were isolated and their molecular masses estimated by mass spectrometry and SDS-PAGE under denaturing conditions. The SVTLEs isolated from B. alternatus (BaIII-3 - 8) and B. moojeni (BmIII-2 - 5) fractions displayed apparent molecular mass around 30-40 kDa which closely relates to SVTLEs from other Bothrops species, as well their amino acid partial sequence triptych ions. Analysis of the alignment of the amino acid residue sequences of the N-terminal of the isolated proteins revealed a high level of identity with other SVTLEs. These enzymes coagulated plasma and showed fibrinogenolytic activity in blood. These SVTLEs isolated can be considered α-fibrinogenase mainly due to the fact that they hydrolyze the Aα chain fibrinogen. B. moojeni SVTLE showed greater activity than those from B. alternatus isolated. This new purification alternative approach developed was faster and more economical than the traditional process currently used. Faster purification and improved extraction yield can provide new insights into these enzymes including the use as a candidate molecule in the production of new drugs.},
year = {2021}
}
TY - JOUR T1 - A Novel Fast and Efficient Approach to Purify the Thrombin-like Enzyme from Two Bothrops-genus Snake Venoms AU - Mauricio Aurelio Gomes Heleno AU - Edda Evnet Newball-Noriega AU - Salomón Huancahuire-Vega AU - Rui Seabra Ferreira Júnior AU - Benedito Barraviera Y1 - 2021/08/31 PY - 2021 N1 - https://doi.org/10.11648/j.ajbls.20210904.15 DO - 10.11648/j.ajbls.20210904.15 T2 - American Journal of Biomedical and Life Sciences JF - American Journal of Biomedical and Life Sciences JO - American Journal of Biomedical and Life Sciences SP - 209 EP - 218 PB - Science Publishing Group SN - 2330-880X UR - https://doi.org/10.11648/j.ajbls.20210904.15 AB - Snake venoms are important sources of complex substances with a variety of pharmacological activities. Among them serine proteinases (SVSPs) have important effects on the hemostatic system influencing the hemodynamic of human or animal blood. Bothrops genus-snake venoms are rich in the thrombin-like enzyme, a type of SVSPs, with great interest to produce medicine. Therefore, the aim of this work was to describe a rapid, only two-step chromatographic-procedure developed to perform a faster purification of SVSPs from Bothrops alternatus and Bothrops moojeni venoms. As a result, two groups of serine proteinases respectively BaIII-4 - 8 and BmIII-2 - 5, were isolated and their molecular masses estimated by mass spectrometry and SDS-PAGE under denaturing conditions. The SVTLEs isolated from B. alternatus (BaIII-3 - 8) and B. moojeni (BmIII-2 - 5) fractions displayed apparent molecular mass around 30-40 kDa which closely relates to SVTLEs from other Bothrops species, as well their amino acid partial sequence triptych ions. Analysis of the alignment of the amino acid residue sequences of the N-terminal of the isolated proteins revealed a high level of identity with other SVTLEs. These enzymes coagulated plasma and showed fibrinogenolytic activity in blood. These SVTLEs isolated can be considered α-fibrinogenase mainly due to the fact that they hydrolyze the Aα chain fibrinogen. B. moojeni SVTLE showed greater activity than those from B. alternatus isolated. This new purification alternative approach developed was faster and more economical than the traditional process currently used. Faster purification and improved extraction yield can provide new insights into these enzymes including the use as a candidate molecule in the production of new drugs. VL - 9 IS - 4 ER -
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