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Isolation of phospholipase A1 from Trypanosoma brucei
Tropenmedizin Und Parasitologie
|March 1, 1984
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.