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Article
The purification of α1-antichymotrypsin from human serum using DNA-cellulose chromatography
Archives of Biochemistry and Biophysics
  • Munir Abdullah, Aga Khan University
  • Anwar Ali Siddiqui, Aga Khan University
  • J Alan Hill, Aga Khan University
  • R Jeremy, Aga Khan University
Publication Date
3-30-1983
Document Type
Article
Abstract
Abstract By exploiting its capacity for binding to DNA, the protease inhibitor α1-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 α1-antichymotrypsin in terms of overall yield and practical convenience. The purified α1-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
Citation Information
Munir Abdullah, Anwar Ali Siddiqui, J Alan Hill and R Jeremy. "The purification of α1-antichymotrypsin from human serum using DNA-cellulose chromatography" Archives of Biochemistry and Biophysics Vol. 225 Iss. 1 (1983) p. 306 - 312
Available at: http://works.bepress.com/anwar_siddiqui/3/