title: Dissociation of lactate dehydrogenase in aqueous and reversed micellar solutions. A time-resolved polarized fluorescence study.
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.
authors.affiliation: Department of Biochemistry, Agricultural University, Wageningen, The Netherlands.
authors.forename: Y L
authors.initials: YL
authors.lastname: Khmelnitsky
authors.forename: A
authors.initials: A
authors.lastname: van Hoek
authors.forename: C
authors.initials: C
authors.lastname: Veeger
authors.forename: A J
authors.initials: AJ
authors.lastname: Visser
mesh_terms: D000818:Animals; D005454:Fluorescence Polarization; D007770:L-Lactate Dehydrogenase / Q000737:chemistry*; D008823:Micelles; D012995:Solubility; D013552:Swine
chemical_list: D008823:Micelles; D007770:L-Lactate Dehydrogenase