A procedure is described for the preparation of crystalline carboxypeptidase Aa from acetone powders of bovine pancreatic tissue. The method involves the isolation of the zymogen by chromatography, activation with trypsin, and dialysis of the activation mixture. One or two recrystallizations suffice to yield a product of maximum specific activity. The procedure is considerably simpler than those previously described and offers the advantage of as much as a 12-fold increase in yield.

No abstract

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