Identification of isoenzyme C as the principal carbonic anhydrase in human ciliary processes.
P. C. Dobbs, David L. Epstein, Peter J. Anderson
Abstract
P. C. Dobbs, David L. Epstein, Peter J. Anderson
Abstract
Carbonic anhydrase was extracted from the excised processes of the ciliary bodies of 10 pairs of enucleated human eyes, and the isoenzyme composition was assayed by measuring the degree of inhibition produced by acetazolamide at two standard concentrations. Also, the effect of incubating with iodoacetate was determined in two pairs of these eyes. Only isoenzyme C was detected. Accordingly, it seems that differences in reduction of intraocular pressure that are common among patients treated for glaucoma with systemic carbonic anhydrase inhibitors, despite uniform serum concentrations, are not attributable to interindividual variation of carbonic anhydrase isoenzymes in the ciliary processes.
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Carbonic anhydrase was extracted from the excised processes of the ciliary bodies of 10 pairs of enucleated human eyes, and the isoenzyme composition was assayed by measuring the degree of inhibition produced by acetazolamide at two standard concentrations. Also, the effect of incubating with iodoacetate was determined in two pairs of these eyes. Only isoenzyme C was detected. Accordingly, it seems that differences in reduction of intraocular pressure that are common among patients treated for glaucoma with systemic carbonic anhydrase inhibitors, despite uniform serum concentrations, are not attributable to interindividual variation of carbonic anhydrase isoenzymes in the ciliary processes.
Key concepts: Acetazolamide, Carbonic anhydrase, Isozyme, Ciliary processes, Carbonic anhydrase inhibitor, Chemistry, Biochemistry, Enzyme