Abstract
A simple, rapid method is described for the preparation of cytochrome c peroxidase from baker's yeast. The procedure involves lysis of the yeast in the presence of ethyl acetate, extraction of the peroxidase in 0.05 M sodium acetate buffer, pH 5.0, and the concentration of the crude extract on a DEAE-agarose column. The DEAE eluate is further concentrated by ultrafiltration, and gel filtration of the concentrate results in a highly purified form of the enzyme. Consistent yields with 80% recovery are easily obtained. Protein isolated by this method in the presence or absence of the protease inhibitor, phenylmethylsulfonyl fluoride (PMSF), contains purely high-spin Fe(III) heme as monitored by its resonance Raman spectrum.
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