The effect of urea on subunit interactions of ß-galactosidase from Escherichia coli K12
作者： Sidney Shifrin , Edward Steers
DOI: 10.1016/0005-2795(67)90550-8
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摘要: Abstract The effect of increasing concentrations urea on sedimentation velocity, enzymatic activity, antigenicity, and protein fluorescence s-galactosidase (s- d -galactoside galactohydrolase, EC 3.2.1.23) indicates that the enzymatically active tetramer is completely dissociated into inactive monomer in 6 M urea. Removal by dialysis results reaggregation to together with a return normal values those properties which have been studied. Protein immunologically related but incapable forming an was added wild-type enzyme presence 8 After renaturation, found be hybrid consisting mutant subunits containing full activity.
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