Preferential solvent interactions between proteins and polyethylene glycols.
نویسندگان
چکیده
منابع مشابه
Mechanism of Precipitation of Proteins by Polyethylene Glycols
The apparent solubilities of various proteins (14,000 to 670,000 daltons) were measured in the presence of polyethylene glycols (PEGS) of different sizes. All of the solubility curves, determined by measur ing the protein concentration in the supernate of centrifuged mixtures, exhibited the characteristic linear dependence of log S (g/liter) on PEG concentration (%, w/v). For human albumin in P...
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Mono-, di-, tri-, and tetraethylene glycols and polyethylene glycols (PEG) with molecular weight up to 20,000 were degraded by soil microorganisms. A strain of Pseudomonas aeruginosa able to use a PEG of average molecular weight 20,000 was isolated from soil. Washed cells oxidized mono- and tetraethylene glycols, but O2 consumption was not detectable when such cells were incubated for short per...
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Solvent additives (cosolvents, osmolytes) modulate biochemical reactions if, during the course of the reaction, there is a change in preferential interactions of solvent components with the reacting system. Preferential interactions can be expressed in terms of preferential binding of the cosolvent or its preferential exclusion (preferential hydration). The driving force is the perturbation by ...
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The apparent solubilities of various proteins (14,000 to 670,000 daltons) were measured in the presence of polyethylene glycols (PEGs) of different sizes. All of the solubility curves, determined by measuring the protein concentration in the supernate of centrifuged mixtures, exhibited the characteristic linear dependence of log S (g/liter) on PEG concentration (%, w/v). For human albumin in PE...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1981
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(19)70019-2