Tan N H
Biochim Biophys Acta. 1982 Aug 27;717(3):503-8. doi: 10.1016/0304-4165(82)90294-x.
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.