super(13)C and super(15)N NMR and time-resolved fluorescence depolarization study of bovine carbonic anhydrase - 4-methylbenzene-sulfonamide complex
The influence of the binding of the high-affinity inhibitor, 4-methylbenzene-sulfonamide to the active site of bovine carbonic anhydrase B was studied by super(15)N- and super(13)C-NMR spectroscopy. The rotational correlation time dependence on temperature and concentration of the complex was determ...
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Veröffentlicht in: | European journal of biochemistry 1989-01, Vol.186 (1-2), p.287-290 |
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