Publication | Open Access
The cold‐induced denaturation of lactate dehydrogenase at sub‐zero temperatures in the absence of perturbants
48
Citations
20
References
1989
Year
Protein ChemistryCold-induced DenaturationAldehyde DehydrogenaseBiochemistryBioenergeticsProtein FoldingLactate DehydrogenaseNatural SciencesMolecular BiologyCold‐induced DenaturationProtein RefoldingCooled Protein SolutionStructure-function Enzyme KineticsMetabolismMedicineAlcohol DehydrogenasesSub‐zero Temperatures
The cold-induced denaturation of lactate dehydrogenase has been determined in an unfrozen, cryoprotectant free solution at sub-zero temperatures. The cold-induced denaturation temperature (TL) has been found to be -28 degrees C. The results for the first time clearly establish that temperature alone can induce denaturation in a cooled protein solution. The validity of earlier data, obtained in the presence of perturbants (particularly pH or guanidinium chloride), is discussed.
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