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The pH Dependence of Serpin-Proteinase Complex Dissociation Reveals a Mechanism of Complex Stabilization Involving Inactive and Active Conformational States of the Proteinase Which Are Perturbable by
Serpin family protein proteinase inhibitors trap proteinases at the acyl-intermediate stage of cleavage of the serpin as a proteinase substrate by undergoing a dramatic conformational change, whichExpand
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Catalysis by the large subunit of the second beta-galactosidase of Escherichia coli in the absence of the small subunit.
Plasmids containing the ebgAo and ebgAa genes of Escherichia coli under the control of the lac repressor and promoter have been constructed and inserted into Salmonella typhimurium CH3. This systemExpand
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Larger increases in sensitivity to paracatalytic inactivation than in catalytic competence during experimental evolution of the second beta-galactosidase of Escherichia coli.
Second-order rate constants (M-1.s-1) at 25 degrees C and pH 7.5 for inactivation of first-generation (ebga and ebgb), second-generation (ebgab and ebgabcd) and third-generation (ebgabcde)Expand
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