TY - JOUR
T1 - Comparison of the venom composition of Bothrops asper, Bothrocophias myersi, Crotalus durissus and Lachesis muta snakes species, from Andina region in Colombia
AU - Sarmiento Acuña, Karen Solanyi
AU - Castiblanco, Ana
AU - Scovino, Stefano
AU - Galvis, Carlos Andrés
AU - Aristizabal, Fabio
PY - 2020/4
Y1 - 2020/4
N2 - The snake´s venoms are the secretions with higher enzymes and toxins in nature, their composition is variable interspecies and intraspecies, even in the same region. Our purpose was compared the protein composition of Bothrops asper, Bothrocophias myersi, Crotalus durissus and Lachesis muta venoms, from Andina region from Colombia. The venoms pool was obtained by agreement with the Fundación Zoológico de Cali, by manual extraction, lyophilized and refrigerated. The project was approval of ethical committee of the Universidad El Bosque and the Instituto de Biotecnología of the Universidad Nacional de Colombia. The venoms protein was quantified by spectrophotometry using the Bradford, Lowry and Nanodrop® methods. The protein composition were made by high efficiency liquid chromatography (HPLC), using a Lichosper 100 RP c18 column of dimensions 250X4 mm, pore size of 5um and by polyacrylamide gel electrophoresis (SDS PAGE). The higher protein was found in Bothrocophias myersi, and Crotalus durissus venoms with 108,6 mg/mL and 78,1 mg/mL respectively. For the four venoms was found fractions between 35-36 minutes and fractions between 0-5minutes, the lower was 1,7 for Bothrocophias myersi and the higher was 3,8 for Crotalus durissus. All venoms showing more than 50% of proteins of 15, 20 and 50KDa. We found characteristics peaks for Bothrops asper at 25 minute, Bothrocophias myersi at 38min and Lachesis muta at 62min. Also, Crotalus durissus and Bothrocophias myersi showed peaks of 100 and 120 KDa, while Crotalus durissus and Lachesis muta showed peaks of 150KD. We conclude the higher protein quantification was for Bothrocophias myersi, the fractions weight was the similar point and they showed few differences in the chromatography characteristics peaks per venom.
AB - The snake´s venoms are the secretions with higher enzymes and toxins in nature, their composition is variable interspecies and intraspecies, even in the same region. Our purpose was compared the protein composition of Bothrops asper, Bothrocophias myersi, Crotalus durissus and Lachesis muta venoms, from Andina region from Colombia. The venoms pool was obtained by agreement with the Fundación Zoológico de Cali, by manual extraction, lyophilized and refrigerated. The project was approval of ethical committee of the Universidad El Bosque and the Instituto de Biotecnología of the Universidad Nacional de Colombia. The venoms protein was quantified by spectrophotometry using the Bradford, Lowry and Nanodrop® methods. The protein composition were made by high efficiency liquid chromatography (HPLC), using a Lichosper 100 RP c18 column of dimensions 250X4 mm, pore size of 5um and by polyacrylamide gel electrophoresis (SDS PAGE). The higher protein was found in Bothrocophias myersi, and Crotalus durissus venoms with 108,6 mg/mL and 78,1 mg/mL respectively. For the four venoms was found fractions between 35-36 minutes and fractions between 0-5minutes, the lower was 1,7 for Bothrocophias myersi and the higher was 3,8 for Crotalus durissus. All venoms showing more than 50% of proteins of 15, 20 and 50KDa. We found characteristics peaks for Bothrops asper at 25 minute, Bothrocophias myersi at 38min and Lachesis muta at 62min. Also, Crotalus durissus and Bothrocophias myersi showed peaks of 100 and 120 KDa, while Crotalus durissus and Lachesis muta showed peaks of 150KD. We conclude the higher protein quantification was for Bothrocophias myersi, the fractions weight was the similar point and they showed few differences in the chromatography characteristics peaks per venom.
UR - http://dx.doi.org/10.1016/j.toxicon.2019.12.024
U2 - 10.1016/j.toxicon.2019.12.024
DO - 10.1016/j.toxicon.2019.12.024
M3 - Article
SN - 0041-0101
VL - 177
SP - S27-S28
JO - Toxicon
JF - Toxicon
IS - S1
ER -