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A new affinity adsorbent for the purification of phospholipases A1 and A2 from animal venoms
J Vargas-Villarreal1, J J Martin-Polo, E Reynaud
1Centro de Investigación sobre Ingeniería Genética y Biotecnología, Universidad Nacional Autónoma de México, Cuernavaca.
Abstract:
Dimethyl-DL-2,3-distearoyloxy-propyl-2'-hydroxy-ethylammonium++ + (Rosenthal's inhibitor) was coupled to carboxyhexyl-Sepharose 4B, through carbodiimide chemistry. Phospholipase A2 from Heloderma horridum horridum and Crotalus adamanteus bind to the immobilized ligand in the presence of Ca2+ and can be easily eluted under acidic conditions or in the presence of a chelating agent, respectively. This affinity media proved to be effective also in the purification of a Ca2(+)-independent phospholipase A1 from vespid venom.