Reversible effects of cross-linking on the regulatory cooperativity of Acinetobacter citrate synthase |
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Authors: | Colin G Mitchell PDJ Weitzman |
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Institution: | Department of Biochemistry, University of Bath, Bath BA2 7AY, England |
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Abstract: | Citrate synthase was purified from Acinetobacter calcoaceticus and treated with the cleavable cross-linking reagent dithiobis(succinimidyl propionate). Cross-linking of the enzyme resulted in the abolition of the sigmoidal responses to inhibition by NADH and re-activation by AMP displayed by the native enzyme. Inhibition and re-activation were still observed but without any cooperativity. Cleavage of the disulphide bonds in the cross-links by treatment with dithiothreitol restored the sigmoidal characteristics of both inhibition and re-activation. |
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Keywords: | Citrate synthase Cross-linking Cooperativity Allosteric regulation Dithiobis(succinimidyl propionate) |
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