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Interaction of Aromatic Amines with Rat Liver Proteins in Vivo

I. PREFERENTIAL LABELING OF A CYTOPLASMIC PROTEIN OR PROTEINS BY N-2-FLUORENYLACETAMIDE-9-¹⁴C

From the ¹ From the Laboratory for Cancer Research, Veterans Administration Hospital, and the Department of Biochemistry, University of Minnesota, Minneapolis, Minnesota 55417

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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