super(13)C and super(15)N NMR and time-resolved fluorescence depolarization study of bovine carbonic anhydrase - 4-methylbenzene-sulfonamide complex

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
Hauptverfasser: Jarvet, J, Olivson, A, Mets, U, Pooga, M, Aguraiuja, R, Lippmaa, E
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cattle
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container_issue 1-2
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container_title European journal of biochemistry
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creator Jarvet, J
Olivson, A
Mets, U
Pooga, M
Aguraiuja, R
Lippmaa, E
description 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 determined by time-resolved fluorescence depolarization measurements. Our experiment provides evidence that the stoichiometry of the interaction of 4-methylbenzene-sulfonamide with carbonic anhydrase B is 1:1 and the inhibitor is bound in anionic form.
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title super(13)C and super(15)N NMR and time-resolved fluorescence depolarization study of bovine carbonic anhydrase - 4-methylbenzene-sulfonamide complex
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