A New Method for Purification of Carbonic Anhydrase Isozymes by Affinity Chromatography

O. Ozensoy¹, O. Arslan^1*, and S. Oznur Sinan²

¹Balikesir University, Science and Art Faculty, Department of Chemistry/Biochemistry Section, 10100 Balikesir, Turkey; fax: 90-266-2493360; E-mail: oktay@balikesir.edu.tr

²Balikesir University, Science and Art Faculty, Department of Biology/Biochemistry Section, 10100 Balikesir, Turkey

^* To whom correspondence should be addressed.

Received March 28, 2003; Revision received November 5, 2003

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A new affinity gel for purification of carbonic anhydrase isozymes was prepared using EUPERGIT^R C-250L derivatized with p-aminobenzenesulfonamide, an inhibitor of carbonic anhydrase. The binding capacity of the affinity gel was determined at different temperatures, pH values, elution buffers, and ionic strengths. Human carbonic anhydrase isozymes (HCA I and HCA II) and bovine carbonic anhydrase (BCA) were purified in high yields from erythrocytes.

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KEY WORDS: EUPERGIT^R C-250L, carbonic anhydrase, affinity chromatography

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