Electron spin resonance studies on cobalt carbonic anhydrase-substrate complexes
TURKISH JOURNAL OF CHEMISTRY, cilt.21, sa.2, ss.134-138, 1997 (SCI-Expanded, Scopus, TRDizin)
- Yayın Türü: Makale / Tam Makale
- Cilt numarası: 21 Sayı: 2
- Basım Tarihi: 1997
- Dergi Adı: TURKISH JOURNAL OF CHEMISTRY
- Derginin Tarandığı İndeksler: Science Citation Index Expanded (SCI-EXPANDED), Scopus, TR DİZİN (ULAKBİM)
- Sayfa Sayıları: ss.134-138
- Anahtar Kelimeler: bovine carbonic anhydrase, ESR spectroscopy, substrate complexes, BINDING, MECHANISM, ZINC, SITE
- Atatürk Üniversitesi Adresli: Evet
Özet
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.