Chromatographic and electrophoretic methods related to the carbonic anhydrase isozymes.
There are three gene families that encode zinc metalloenzymes that catalyze the reversible hydration of CO2. The encoded enzymes are termed carbonic anhydrases (CAs). The CA isozymes have been purified from representatives of all types of organisms. Most CAs are strongly inhibited by aromatic sulfonamides. Several chromatographic and electrophoretic methods have been devised to determine binding constants for sulfonamides to CAs, and these compounds have been extensively used for, often single-step, affinity chromatographic separation of CAs from complex matrixes. The purification of different CA isozymes from different organisms is reviewed, as are methods for detection of CAs during chromatography and electrophoresis.
Bergenhem
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Department of Biological Chemistry, University of Michigan, Abn Arbor 48109-2007, USA.
D000818:Animals; D002256:Carbonic Anhydrases / Q000032:analysis* / Q000302:isolation & purification / Q000378:metabolism; D002853:Chromatography, Liquid / Q000379:methods*; D004591:Electrophoresis, Polyacrylamide Gel / Q000379:methods*; D006801:Humans; D008322:Mammals
D002256:Carbonic Anhydrases