Carbonic Anhydrase I from human erythrocytes

Carbonic anhydrase from human erythrocytes (HCA) has been used to study the molten-globule state of carbonic anhydrase (CA). Chaperone-like α-crystallin binds to this state of the enzyme and prevents its aggregation. The enzyme from sigma has been used for the analysis of thermodynamic stability of the enzyme. Furthermore, its clinical significance has been evaluated in human non-small cell lung cancer.

Carbonic anhydrase is a zinc metalloenzyme that has a molecular weight of approximately 30,000 Da. The enzyme catalyzes the hydration of carbon dioxide to carbonic acid. It is involved in vital processes such as pH and CO₂ homeostasis, transport of bicarbonate and CO₂, biosynthetic reactions, bone resorption, calcification, and tumorigenicity. Therefore, this enzyme is an important target for inhibitors with clinical applications in various pathologies such as glaucoma, epilepsy and Parkinson′s disease.

chromatographically
purified.

One Wilbur-Anderson (W-A) unit will cause the pH of a 0.02 M Trizma buffer to drop from 8.3 to 6.3 per min at 0 °C. (One W-A unit is essentially equivalent to one Roughton-Booth unit.)