Purification of phospholipase c from pseudomonas fluorescens by chromatography on 2-(4-aminophenyl-sulphonyl)ethyl-cellulose

Abstract

Phosphatidylcholine-specific phospholipase C (PC-PLC) was purified 1875 fold from the culture medium of Pseudomonas fluorescens strain D. The purification procedure was based on the enzyme affinity to 2-(4-aminophenylsulphonyl)ethyl-cellulose. The purified PLC appeared as a single band after SDS PAGE. Pseudomonas fluorescens phospholipase C was terminally blocked. The sequence of the enzyme, secreted by P. fluorescens strain D apparently was not identical to that reported by Preuss et al. (24). © 2003 Taylor and Francis Group, LLC.