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Characterization of cobalt(II) bovine carbonic anhydrase and of its derivatives

✍ Scribed by Bertini, I.; Canti, G.; Luchinat, C.; Scozzafava, A.


Book ID
120485876
Publisher
American Chemical Society
Year
1978
Tongue
English
Weight
584 KB
Volume
100
Category
Article
ISSN
0002-7863

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πŸ“œ SIMILAR VOLUMES


Characterization of nickel(II) bovine ca
✍ I. Bertini; E. Borghi; C. Luchinat πŸ“‚ Article πŸ“… 1978 πŸ› Elsevier Science βš– 589 KB

The nickel(II) derivative of carbonic anhydrase and its adducts with inhii itors have been investigated through electronic and nuclear magnetic resonance (mnrj spectroscopy. The metal ion in the pure enzyme is six-coordinated, and the\* is evidence for at least one water molecule in the coordination

Binding affinity of bicarboxylate ions f
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The affinity of bicarboxylate ions (from oxaiate to glutarate) for cobalt(E) bovine carbonic anhydrase has been investigated and compared with that cf acetate and propionate. The oxalate ion shows a much greater affiiity for the enzyme than acetate. whereas the other bicarboxylate ions have very lit

Interactions between Ξ±-amino acids and c
✍ I. Bertini; C. Luchinat; A. Scozzafava πŸ“‚ Article πŸ“… 1977 πŸ› Elsevier Science βš– 426 KB

The results of a study on the interaction between cobalt(II) bovine carbonic anhydrase and the a-amino acids L(s) and D(-Manine. glycine and betaine are reported\_ L(+)ahnine and glycine base been found to have larger aftinity for the enzyme than II(-) alanine whereas no sizable affinity is shown by

Denaturation of cobalt–carbonic anhydras
✍ Leslie F. McCoy Jr.; Kin-Ping Wong πŸ“‚ Article πŸ“… 1979 πŸ› Wiley (John Wiley & Sons) 🌐 English βš– 703 KB

## Abstract We have attempted to elucidate the mechanism of the acquisition of active‐site conformation in enzymes by studying the unfolding and refolding of Co(II) carbonic anhydrase. This enzyme possesses characteristic absorption and CD spectra in the visible region, which reflect primarily the