• Corpus ID: 29384185

113Cd nuclear magnetic resonance of mammalian erythrocyte carbonic anhydrases.

  title={113Cd nuclear magnetic resonance of mammalian erythrocyte carbonic anhydrases.},
  author={Antonius J.M. Schoot Uiterkamp and Ian M. Armitage and Joseph E. Coleman},
  journal={The Journal of biological chemistry},
  volume={255 9},
113Cd NMR of the 113Cd(II)-substituted zinc metalloenzymes, human and bovine erythrocyte carbonic anhydrases, is reported. The high activity isozymes, human erythrocyte carbonic anhydrase, isozyme C (HCAC) and bovine erythrocyte carbonic anhydrase, isozyme B (BCAB), are characterized by relatively narrow 113Cd resonances around 220 ppm to lowfield of Cd(ClO4)2. These resonances are relatively invariant between pH 5.5 and 10. In contrast, the low activity isozyme, human carbonic anhydrase B… 
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