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
Recommended Citation
NUHOĞLU, Çigdem; DEMİR, Nazan; NALBANTOĞLU, Barbaros; KÜFREVİOĞLU, Ö. İrfan; YOĞURTÇU, Y. Kemal; ÖZDEMİR, Hasan; and AYYILDIZ, Enise (1997) "Electron Spin Resonance Studies on Cobalt Carbonic Anhydrase-Substrate Complexes," Turkish Journal of Chemistry: Vol. 21: No. 2, Article 10. Available at: https://journals.tubitak.gov.tr/chem/vol21/iss2/10