Purification and properties of carbonic anhydrase from salmon erythrocytes.
Carbonic anhydrase (CA) from erythrocytes of the pink salmon, Onchorhyncus gorbushka, was purified using chloroform-ethanol extraction and Sephadex G-75 gel filtration. A single, high specific-activity CA isozyme having a molecular weight of 29,000 was found. The enzyme sedimented as a single boundary at a sedimentation velocity of 2.9S. Amino acid analysis revealed a composition similar to other submammalian CAs with the exception that the cysteine content was low (1 mol cysteine/mol enzyme). Like other submammalian CAs, the presence of a sulfhydryl reducing agent was required to maintain full activity and to prevent structural changes in the enzyme.
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002256:Carbonic Anhydrases / Q000097:blood* / Q000302:isolation & purification; D004228:Dithionitrobenzoic Acid / Q000494:pharmacology; D004912:Erythrocytes / Q000201:enzymology*; D007700:Kinetics; D008970:Molecular Weight; D012474:Salmon; D013045:Species Specificity
D000596:Amino Acids; D004228:Dithionitrobenzoic Acid; D002256:Carbonic Anhydrases