Abstract
An acidic phospholipase A 2 from cod muscle was partially purified by anion exchange chromatography, precipitation by acidification, and chromatofocusing. The molecular weight was estimated to be over 50 kDa and the isoelectric point was determined to be about 5.2. The pH optimum of this enzyme was 4.0 and the activity had a temperature optimum at 40°C. The activity was not dependent on free calcium ions.
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