Strategic modifications were introduced on current antivenom immunization schedules allowing production of high specific-affinity-toxin neutralizing IgG and IgY polyclonal antibodies (Abs). Crotalus durissus terrificus phospholipase A2 (PLA2), Bitis arietans Kn-Ba serine protease, expressing fibrinolytic activity both on α and β fibrinogen or on synthetic Met-Lys-bradykininogen with bradykinin release, an angiotensin-converting enzyme I (ACE-I) present in Tityus. serrulatus venom, were purified and biologically characterized to be used as substitutes for crude venom in immunization procedures. Anti-toxins monoclonal Abs (mAbs) are in development. The pAbs/mAbs hypervariable regions are being used as complementarity-determining region (CDRs) sequence sources. IgY anti-snake venom toxin CDRs were isolated, sequenced and used for molecular modeling. In conclusion, improvements on currently used antivenoms therapeutic qualities were accomplished.