Isolation of phospholipase A1 from Trypanosoma brucei.

Abstract

Phospholipase A1 from Trypanosoma brucei brucei has been purified 380-fold by column chromatography on phosphatidylcholine-Sepharose affinity columns followed by DEAE-cellulose anion-exchange chromatography and Sephacryl S-200 molecular exclusion chromatography. Octyl-Agarose hydrophobic column chromatography can be substituted for the PC-Sepharose column. The molecular weight of trypanosomal PLase A1 was found to be 26,000 by SDS-polyacrylamide gel electrophoresis.