Electron spin resonance studies on cobalt carbonic anhydrase-substrate complexes

NUHOGLU C., DEMIR N., NALBANTOGLU B., KUFREVIOGLU O., YOGURTCU Y., Ozdemir H., ...Daha Fazla

TURKISH JOURNAL OF CHEMISTRY, cilt.21, sa.2, ss.134-138, 1997 (SCI-Expanded) identifier identifier

  • 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.