Indexed on: 01 Mar '74Published on: 01 Mar '74Published in: Experientia
The isolation of carbonic anhydrase from hen's egg shells is reported. The enzyme has been purified by gelfiltration and ion-exchange chromatography. The elution pattern of carbonic anhydrase from egg shells differs remarkably from that of enzyme preparations of erythrocytes. The purified enzyme catalyzed the reversible hydration of CO2 and aldehydes as well as the hydrolysis ofp-nitrophenyl acetate. Deletion of 2-mercaptoethanol from extraction and elution buffer solutions caused a complete loss of carbonic anhydrase activity, as did the addition ofp-mercuribenzoate. The biological significance of the occurance of carbonic anhydrase in the hen's egg shell is discussed.