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Dissociation of lactate dehydrogenase in aqueous and reversed micellar solutions. A time-resolved polarized
Y L Khmelnitsky1, A van Hoek, C Veeger
1Department of Biochemistry, Agricultural University, Wageningen, The Netherlands.
Abstract:
Dissociation behavior of lactate dehydrogenase from hog muscle, both in aqueous solution and reversed micelles of sodium bis(2-ethylhexyl sulfosuccinate) in octane was studied using time-resolved polarized fluorescence spectroscopy. It was found that, in aqueous solutions, the enzyme underwent partial dissociation with the formation of isolated subunits at enzyme concentrations below 8 nM. Dissociation of the enzyme also took place upon entrapment of lactate dehydrogenase into reversed micelles under conditions of low surfactant hydration, when micelles were not large enough to accommodate a whole protein molecule.