Turkish Journal of Chemistry
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.
Bovine carbonic anhydrase, ESR spectroscopy, substrate complexes.
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