Abstract
Toyopearl media for gel filtration tend to adsorb proteins at high ionic strength, presumably by hydrogen bonding. This is used in the technique proposed here for resolution of crude protein mixtures and initial purification of their components. Proteins can be selectively adsorbed on a column of Toyopearl at high ammonium sulfate concentration and then eluted by decreasing the salt concentration. This single-step procedure can replace the usual salt fractionation of protein mixtures, which is demonstrated with yeast cytochrome oxidase.
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