Table 1.
Lots of the antivenoms included in the present study.
Table 2.
Results of protein quantification of antivenoms.
Fig 1.
12.5% SDS-PAGE of the antivenoms.
Migration was performed under reducing conditions, 25 μg of protein was loaded in each lane, and control with F(ab’)2 + equine albumin fragments was included.
Fig 2.
Percentage of specific F(ab’)2 fragments contained in the antivenoms.
Fig 3.
A) Reducing conditions; B) Non-reducing conditions. Lane 1, Agkistrodon bilineatus; 2, Bothrops asper; 3, Cerrophidion tzotzilorum; 4, Crotalus atrox; 5, Crotalus basiliscus; 6, Crotalus mictlantecuhtli; 7, Metlapilcoatlus nummifer; 8, Ophryacus sphenophrys; 9, Porthidium yucatanicum.
Fig 4.
RP-HPLC chromatograms were obtained for the affinity assays.
In each graph, 3 chromatograms are shown superimposed: complete venom, recognized fraction, and unrecognized fraction in black, blue, and red, respectively. In addition, the percentage of acetonitrile (B) is shown with a dotted line. The level of recognition toward the venoms of B. asper, C. atrox, and C. mictlantecuhtli was evaluated for Antivipmyn batch A1, Birmex B1, and Inoserp I1.
Fig 5.
Western blot of the resin where the venom was retained.
Lane 1, CNBrS-Antivipmyn batch A1; 2, mixture of Crotalus atrox venom and Antivipmyn A1; 3, Antivipmyn A1; 4, Crotalus atrox venom; 5, CNBrS- Antivipmyn A1 after incubation with Crotalus atrox venom.
Table 3.
Neutralization of lethal activity.
Table 4.
Neutralization of proteolytic activity.
Table 5.
In vitro fibrinogenolytic activity and its neutralization.
Fig 6.
Neutralized LD50 values per vial.
Error bars correspond to 95% confidence intervals. The dotted line represents the minimum neutralization established by the NOM-036-SSA2-2012. *, the lethal activity was not neutralized even with the highest antivenom administered.