Turkish Journal of Medical Sciences
The Inhibition Kinetics of Bovine and Human Erythrocyte Carbonic Anhydrase Isozymes with Some Active Cations
DOI
-
Abstract
In this study, the in vitro effects of some active cations on carbonic anhydrase (CA) isozymes were investigated. Bovine (BCA) and human (HCA-I and H CA-ll) isozymes were purified by affinity chromatography from bovine and human erythrocytes. In order to make the kinetic studies, esterase activities of CA isozymes were determined. By using AI{^3+}, Mn{^2+}, Sr{^2+}, Hg{^2+}, Ni{^2+}, Ca{^2+}, and Cd{^2+}ions, K _iconstants for CA isozymes were found by means of Linewear-Burk graphics. While A1{^3+} showed competitive inhibition, the others displayed noncompetitive inhibition. In addition, the inhibitor concentrations halving the enzyme activity (I{_50} values) were determined. The determined I{_50} values for BCA, HCA-I and CA-ll were fit to the obtained Ki values.
Keywords
Carbonic anhydrase, isozymes, active cations, kinetics
First Page
559
Last Page
563
Recommended Citation
ÖZDEMİR, Hasan; KÜFREVİOĞLU, İrfan; NALBANTOĞLU, Barbaros; DEMİR, Nazan; and BAKAN, Nuri (1997) "The Inhibition Kinetics of Bovine and Human Erythrocyte Carbonic Anhydrase Isozymes with Some Active Cations," Turkish Journal of Medical Sciences: Vol. 27: No. 6, Article 12. Available at: https://journals.tubitak.gov.tr/medical/vol27/iss6/12
