Abstract
Aqueous polymer two-phase systems containing dextran T-500 and PEG 4000 can be prepared which are biphasic below 18°C and monophasic at higher temperatures. Both liganded and unliganded forms of glutamate dehydrogenase and troponin, which have similar partition coefficients if the protein is added to a two-phase system at 4°C, have widely differing partition coefficients if added to the same system in the monophasic state at 20°C and subsequently cooled to 4°C.
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