Acidic phospholipases A2 from the venom of common sea snake Enhydrina schistosa.
Two acidic phospholipases A have been purified from the venom of common sea snake (Enhydrina schistosa) by chromatography on Sephadex G-75 gel media, Bio-Rex 70 ion-exchanger followed by repeated Chromatography on DEAE-Sephadex A-25 ion-exchanger. The two preparations were shown to be homogeneous by polyacrylamide gel electrophoresis and ion-exchange chromatography. The enzymes were shown to be specific for the 'two' position of egg yolk lecithin. The molecular weight of both enzymes determined by gel filtration chromatography and SDS-polyacrylamide gel electrophoresis was approx. 14 000. Both enzymes were non-lethal. Amino acid composition data indicated high contents of aspartic acid, glycine and alanine in both enzymes.
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D055598:Chemical Phenomena; D002621:Chemistry; D002850:Chromatography, Gel; D002852:Chromatography, Ion Exchange; D005227:Fatty Acids / Q000032:analysis; D006863:Hydrogen-Ion Concentration; D010740:Phospholipases / Q000302:isolation & purification*; D010741:Phospholipases A / Q000302:isolation & purification*; D012910:Snake Venoms / Q000032:analysis*
D000596:Amino Acids; D005227:Fatty Acids; D012910:Snake Venoms; D010740:Phospholipases; D010741:Phospholipases A