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Turkish Journal of Chemistry

DOI

-

Abstract

The native zinc atom of bovine erythrocyte carbonic anhydrase purified by affinity choromatography was removed by dialysis against pyridine 2,6-dicarboxylic acid. Cobalt carbonic anhydrase was prepared from the zinc-free apoenzyme. The binding conditions of CO_2 and p-nitrophenylacetate to cobalt carbonic anhydrase were investigated by electron spin resonance at different pH levels.

Keywords

Bovine carbonic anhydrase, ESR spectroscopy, substrate complexes.

First Page

134

Last Page

138

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