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Isozymes of Bovine Milk Catalase

Department of Animal Products Science and Technology, Nippon Veterinary and Zootechnical College, Musashino-shi, Tokyo

ABSTRACT

Isozymes of bovine milk catalase were investigated by diethylaminoethyl-Sephacel column chromatography and polyacrylamide gel electrophoresis. Bovine milk catalase was in both cream and skim milk. It was separated and partially purified. When cream catalase was fractionated by diethylaminoethyl-Sephacel column chromatography, two enzymatically active fractions, I and II, were separated by linear sodium gradient elution. They were eluted with .09 M (fraction I) and .33 M (fraction II) sodium chloride. When the catalase of skim milk was eluted with .1 M (fraction III) sodium chloride, it was presented as a single catalase peak.

Further, the electrophoretic characteristics of fractions I to III were examined by polyacrylamide disc gel electrophoresis. As a result, the catalase activity bands of fractions I and II were recognized at a distance of 4 and 11 mm from the starting point. Fraction III was two bands at a distance of 4 and 18 mm. Three apparently different types of catalase are in bovine milk.