Abstract
HYDROPHILIC gels such as those formed from cross-linked dextran–Sephadex−1, agar2 and agarose3 are extensively used for molecular-size dependent fractionation (such as gel filtration and gel permeation chromatography). Although solute-gel interaction other than, or in addition to, molecular sieving are often evident4–6, such interactions have seldom been deliberately exploited for fractionation of protein mixtures. We describe below a method for protein fractionation based on hydrophobic salting-out adsorption in non-ionic amphiphilic gels.
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PORATH, J., SUNDBERG, L., FORNSTEDT, N. et al. Salting-out in Amphiphilic Gels as a New Approach to Hydrophobia Adsorption. Nature 245, 465–466 (1973). https://doi.org/10.1038/245465a0
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DOI: https://doi.org/10.1038/245465a0
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