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- W2010003067 abstract "1. Denaturation of Neurospora crassa pyruvate kinase was investigated using guanidine hydrochloride as a denaturant. 2. The substrates, phosphoenolpyruvate and adenosine diphosphate, stabilize the enzyme against dissociation and structural disorganization, the allosteric activator, fructose 1,6-diphosphate caused an increased destabilization in the presence of the denaturant. 3. Following complete denaturation/unfolding pyruvate kinase was refolded and reactivated, generating a biologically active species showing immunological identity with the native enzyme. 4. For full renaturation and reactivation the allosteric effector and dithiothreitol are required. 5. Studies of pH dependence of renaturation suggest a requirement for the integrity of a residue with a pK around 6.0 for folding and reactivation steps." @default.
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- W2010003067 title "Studies on the structure-function relationships of Neurospora crassa pyruvate kinase: Refolding and reactivation following denaturation in guanidine hydrochloride" @default.
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- W2010003067 doi "https://doi.org/10.1016/0020-711x(81)90138-5" @default.
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