Alkylation of Histidine Residues of Bothrops jararacussu Venom Proteins and Isolated Phospholipases : A Biotechnological Tool to Improve the Production of Antibodies
Figure 3
Cross-reactivity of antibodies produced from native or alkylated proteins BthTX-I and BthTX-II (anti-BthTX-I, anti-alk-BthTX-I, anti-BthTX-II, and anti-alk-BthTX-II) against other isolated PLA2s, as shown by enzyme immunoassay. Lys49-PLA2 homologs (Bothrops jararacussu BthTX-I, B. pirajai PrTX-I and II, B. moojeni MjTX-I and II, B. pauloensis BnSP-6 and 7, and B. asper Basp-II), basic Asp49-PLA2s (B. jararacussu BthTX-II, B. pirajai PrTX-III, B. asper Basp-III, and Crotalus d. terrificus CB), acidic Asp49-PLA2s (B. jararacussu BthA-I-PLA2, B. pirajai BpirPLA2-I, and B. moojeni BmooPLA2-I), and PLA2 from Apis mellifera venom [2–4, 6, 21, 30, 45, 46]. Microplate wells were coated with antigen, and antibody binding was measured, as described in Section 2.5.2. Cross-reactivity was expressed as a percentage of the absorbance signal resulting from the binding of antibodies to the homologous antigen BthTX-I or -II. Crotamine was included as an unrelated, negative control antigen. Results expressed as means ± S.D. ().
