Measurement of protease activity A method has been dareloped for the part@ purification of a c&l-cium activated neutral protease from bovine muscle, since application of methods previously used for rabbit or porcine muscle gave little or no yield. The new method involves extraction with phosphate-buffered KCl, saling out with (NH&SO4, affinity chromatography on mercurial agarose followed by gel filtration. The bovine protease required :alcium ion and reducing agent for activity with a pH optimum at 7.5 and hydrolyzed myofibrillar proteins.Casein digestion was determined using 0.2-l mg enzyme per ml at 25'C by the method described by Kang and Warner (1974)
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