Abstract
1. 1. Carbonic anhydrase was isolated from rabbit erythrocytes by ion-exchange chromatography, isoelectric focusing and affinity chromatography. 2. 2. The low activity (CAI) isoenzyme was purified to homogeneity. 3. 3. The high activity (CAII) enzyme was found to be heterogeneous, yielding at least four enzyme fractions, which reacted with antiserum prepared against one of these forms and which exhibited similar kinetic properties but differed in electrophoretic mobilities and isoelectric points. 4. 4. Both CAI and CAII were partially inhibited by oxidation (i.e. storage in absence of a reducing agent) and by p-chloromercuribenzoate. 5. 5. Antibodies to purified CAI cross-reacted with one fraction of CAII whose specific activity was lower than that of the other CAII preparations, suggesting the presence of a minor form of CAI. 6. 6. Studies of tissue-specific carbonic anhydrases must take into account the existence of multiple forms of the enzyme in the contaminating erythrocytes, as well as possible micro-heterogeneity of the tissue enzyme.
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callMore From: Comparative Biochemistry and Physiology -- Part B: Biochemistry and Molecular Biology
Disclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
