RT Journal Article
SR Electronic
T1 Isolation and Properties of Carbonic Anhydrase from Dog Kidney and Erythrocytes
JF Molecular Pharmacology
JO Mol Pharmacol
FD American Society for Pharmacology and Experimental Therapeutics
SP 142
OP 152
VO 3
IS 2
A1 PAUL BYVOET
A1 AIJA GOTTI
YR 1967
UL http://molpharm.aspetjournals.org/content/3/2/142.abstract
AB DEAE-cellulose chromatography of dog red cell carbonic anhydrase (CA) yielded a single main fraction, whereas under identical conditions human CA showed two distinct activity peaks corresponding with types B and C. When subjected to zone electrophoresis at pH 9.0 or 6.0, the main dog CA fraction moved as a single band with the same mobility as human CA type B. Its Km was found to be approximately 30 mM CO2 at 0°, 50% inhibitory concentrations for acetazolamide and sulfanilamide were similar to those of human CA type C. Structurally the enzyme appeared to be similar to other mammalian CA varieties. Preliminary experiments with CA obtained from the cytoplasmic fraction of dog kidney showed this enzyme to be similar to the red cell enzyme with respect to electrophoretic mobility and inhibition kinetics. ACKNOWLEDGMENTS The authors wish to thank Dr. T. H. Maren for his interest and helpful suggestions. They also acknowledge the excellent assistance of Dr. T. K. McClane, Miss C. E. Wiley, Mr. A. C. Ellison, Mr. R. G. Schaffter, and Mr. R. Stern in various phases of this work. This research was supported by NIH grants CA 18402 and NB 01297.