The proteolytic nature of commercial samples of galactose oxidase. Purification of the enzyme by a simple affinity method.
Several commercially available samples of galactose oxidase (D-galactose: oxygen 6-oxidoreductase, EC 1.1.3.9) were found to contain high proteolytic activity on proteins such as fibrinogen, transferrin, albumin and casein. A simple, efficient method was devised for the purification of galactose oxidase which relies on the affinity of the enzyme for agarose (Sepharose 6B). The purified galactose oxidase was recovered in high yield free from proteolytic activity. The enzymic affinity for Sepharose and Sephadex was investigated to clarify the absorption mechanism.
D000429:Alcohol Oxidoreductases / Q000302:isolation & purification*; D002846:Chromatography, Affinity; D005069:Evaluation Studies as Topic; D005692:Galactose Oxidase / Q000302:isolation & purification* / Q000378:metabolism; D010447:Peptide Hydrolases / Q000302:isolation & purification* / Q000378:metabolism; D011786:Quality Control
D000429:Alcohol Oxidoreductases; D005692:Galactose Oxidase; D010447:Peptide Hydrolases