The purification of alpha 1-antichymotrypsin from human serum using DNA-cellulose chromatography.

By exploiting its capacity for binding to DNA, the protease inhibitor alpha 1-antichymotrypsin has been isolated from human serum by ammonium sulfate fractionation and successive chromatography on QAE-Sephadex, DNA-cellulose, and Sephacryl S-300. This experimental procedure compares favorably with existing methods for preparing alpha 1-antichymotrypsin in terms of overall yield and practical convenience. The purified alpha 1-antichymotrypsin was homogeneous as judged by electrophoretic and immunoelectrophoretic criteria. From its inhibition of the fluorimetric titration of chymotrypsin with 4-methylumbelliferyl-p-trimethylammonium cinnamate it was shown to combine with chymotrypsin in a 1:1 molar ratio and thus to retain its biological activity.