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 .09M (fraction I) and .33M (fraction II) sodium chloride. When the catalase of skim milk was eluted with .1M (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 11mm from the starting point. Fraction III was two bands at a distance of 4 and 18mm. Three apparently different types of catalase are in bovine milk.
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