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