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AI Summary & Key Takeaways
AI Insight⚡ TL;DR(Too Long; Didn't Read)
The binding conditions of CO2 and p-nitrophenylacetate to cobalt carbonic anhydrase were investigated by electron spin resonance at different pH levels.
📌 3 Key Takeaways
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Objective & Hypothesis:The native zinc atom of bovine erythrocyte carbonic anhydrase purified by affinity choromatography was removed by dialysis against pyridine 2,6-dicarboxylic acid.
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Key Findings & Data:Cobalt carbonic anhydrase was prepared from the zinc-free apoenzyme.
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Conclusion & Impact:The binding conditions of CO2 and p-nitrophenylacetate to cobalt carbonic anhydrase were investigated by electron spin resonance at different pH levels.
🔬Design:Research Article
📍Scope:Comprehensive Sample
⚙️Variables:Domain Parameters
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 CO2 and p-nitrophenylacetate to cobalt carbonic anhydrase were investigated by electron spin resonance at different pH levels.
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Cite This Article
DEMİR, N., NUHOĞLU, Ç., NALBANTOĞLU, B., YOĞURTÇU, Y. K., AYYILDIZ, E., KÜFREVİOĞLU, Ö. İ., ÖZDEMİR, H. (2022). Electron spin resonance studies on cobalt carbonic anhydrase-substrate complexes. Turkish Journal of Chemistry, Cilt: 21 - Sayı: 2, 134–138. https://ajindex.com/articles/602610