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C55-Isoprenoid alcohol phosphokinase from Staphylococcus aureus has been purified by the following methods: cooling of a butanol extract to 0° and then to -20° followed by treatment of the dried enzyme with methanol containing increasing amounts of butanol-1. At a concentration of 30% butanol in methanol, enzyme is eluted as a lipoprotein that is purified 627-fold with respect to protein and about 40-fold with respect to lipid phosphate. Qualitative changes in the lipid composition of the purified preparation were demonstrated as well as a simplification of the protein distribution seen on sodium dodecyl sulfate gels. Some properties of this lipoprotein are described. Two more purification steps in organic solvents (chromatography on DEAE-cellulose and chromatography on hydroxypropylated Sephadex G-50) led to apoprotein of near homogeneity. The hydroxypropylated Sephadex G-50 column was shown to separate proteins below molecular weight of 30,000 according to molecular weight. The enzyme activity appeared to be associated with a single polypeptide chain of molecular weight 17,000.
Sandermann et al. (Tue,) studied this question.