Evidence of a high-activity C type of carbonic anhydrase in human ciliary processes.
Carbonic anhydrase activity was found in the ciliary process of fresh human donor eyes, originating from an enzyme antigenically similar to the erythrocyte high-activity isoenzyme HCA C. It was sensitive to inhibition by acetazolamide and resistant to inhibition by halides like HCA C. The enzyme is probably identical with HCA C. Its tissue concentration was one fifth to one tenth of that in the human kidney. The erythrocyte low-activity isoenzyme HCA B was also found in the processes as a contaminant.
D000086:Acetazolamide / Q000494:pharmacology; D000818:Animals; D001639:Bicarbonates / Q000378:metabolism; D002256:Carbonic Anhydrases / Q000032:analysis* / Q000097:blood; D002924:Ciliary Body / Q000187:drug effects / Q000201:enzymology; D006801:Humans; D007527:Isoenzymes / Q000032:analysis* / Q000097:blood; D008565:Membrane Proteins / Q000032:analysis; D011193:Potassium Iodide / Q000494:pharmacology; D011817:Rabbits; D011864:Radioimmunosorbent Test; D012965:Sodium Chloride / Q000494:pharmacology
D001639:Bicarbonates; D007527:Isoenzymes; D008565:Membrane Proteins; D011193:Potassium Iodide; D012965:Sodium Chloride; D002256:Carbonic Anhydrases; D000086:Acetazolamide