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.

Characterization of a high activity carbonic anhydrase isozyme purified from erythrocytes of Salmo gairdneri.

1. A single, high specific activity carbonic anhydrase (CA) isozyme was present in erythrocytes of the teleostean species Salmo gairdneri (rainbow trout). 2.

Lipoidal membranes stabilize isolated salmon and chicken carbonic anhydrase under conditions of increased temperature and pH.

1. Solutions of purified carbonic anhydrase from chicken and salmon erythrocytes were incubated in buffer for 1 hr at 5 degrees or 22 degrees C, at pH 7.3, 7.