A rapid and reproducible chromatographic method for the partial resolution of the basic soluble proteins in rat liver cytoplasm has been devised. The method involves the successive fractionation of the soluble proteins by gel filtration on Sephadex G-25 and by ion exchange chromatography on diethylaminoethyl cellulose. With the use of this method, a weakly basic protein (proteins) has been isolated which binds preferentially a metabolite (metabolites) of the carcinogenic aromatic amide, N-2-fluorenylacetamide-9-14C. The physical properties of this protein (proteins) suggest that it is related to or identical with the h2 proteins isolated from rat liver cytoplasm by means of column electrophoresis by Sorof and his associates.
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Barry et al. (1966) studied this question.
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