Authors: Çigdem NUHOĞLU, Nazan DEMİR, Barbaros NALBANTOĞLU, Ö. İrfan KÜFREVİOĞLU, Y. Kemal YOĞURTÇU, Hasan ÖZDEMİR, Enise AYYILDIZ
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.
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