Carbonic Anhydrase from bovine erythrocytes
lyophilized powder, ?2,000 W-A units/mg protein
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Carbonic anhydrase from bovine erythrocytes (BCA) has been used to study the effect of removal of enzyme-bound metal ion, Zn2+, on aggregation behavior of the enzyme. Removal of metal ion by a chelator such as EDTA enhances the propensity of the enzyme to adopt the molten-globule state. This state of the enzyme is found to bind to the chaperone-like α-crystallin and prevent aggregation. The enzyme from Sigma has been immobilized to electrochemical transducers in order to obtain develop an analytical device for dissolved CO2 measurement. It has also been used for the thermodynamic analysis of conformational changes in BCA.
