Purification and Comparison of Peroxisomal and Cytosolic Catalases from a Methanol-Grown Yeast, Kloeckera sp. 2201

Abstract

Catalases were purified from a peroxisome-containing particulate fraction and a cytosolic fraction of methanol-grown Kloeckera sp. 2201 cells after subcellular fractionation. No difference was observed between the enzymes in the behaviours on column chromatographies, molecular mass of the subunits (M, 62, 000 daltons), and terminal amino acids, alanine. In addition, similar patterns were obtained with the peroxisomal and cytosolic enzymes on sodium dodecylsulfate/polyacrylamide slab-gel electrophoresis of the peptide fragments prepared by partial digestion with Staphylococcus aureus V 8 protease and papain. These results indicate that cytosolic catalase, even if functional, essentially has identical properties with the peroxisomal one in spite of the different subcellular distribution.