Abstract
Catalase is a characteristic enzyme of peroxisomes, of which it is the most abundant protein. This enzyme serves as a typical example of a peroxisomal enzyme and is important in the teaching of biochemistry and molecular biology. Although there is substantial information regarding catalase purification, purifying catalase for the junior‑grade undergraduate experimental course face challenges in obtaining materials and increasingly expensive purification equipment. This study presents a simple method for the purification of mouse liver catalase using ethanol‑chloroform treatment, sodium sulfate fractionation, dialysis and Sephadex G‑200 gel filtration chromatography. Catalase was purified 31.8‑fold with an 18.3% yield. The advantages of this method were its low operating environment requirements, simple procedure and reduced cost. Furthermore, the method was designed to improve students' comprehensive ability and manipulative ability and to introduce a sense of innovation in the fields of biochemistry and molecular biology during their junior year.
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