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Chromatographic Analysis of Cationic Nuclear Proteins of a Number of Neoplastic Tissues^*

Joseph R. Davis^, and Harris Busch

( Department of Pharmacology, University of Illinois College of Medicine, Chicago 12, Ill.)

Radioactive acid-soluble nuclear proteins (histones) of a variety of tumors and of regenerating liver and embryonic tissue have been chromatographed and separated into a number of peaks by gradient elution from carboxymethylcellulose adsorbent with formic acid as the eluting agent. In the tumors studied, including the Jensen sarcoma, Flexner-Jobling carcinoma, Ehrlich ascites tumor, and Sarcoma 180, as well as a human malignant melanoma, 33–45 per cent of the radioactive lysine in the acidsoluble nuclear proteins was found in a peak (RP2-L), which previously was reported to be present in the Walker tumor but not in nontumorous tissues. The peak, RP2-L, was not found in samples of regenerating rat liver or rat embryonic tissue. These data suggest that a qualitative difference exists between tumors and other tissues in biosynthesis of nuclear proteins.

^* These studies were supported in part by grants from the Jane Coffin Childs Fund for Medical Research and the American Cancer Society.

Postdoctoral Fellow of the American Cancer Society.

Present address: Dept. of Pharmacology, Baylor University College of Medicine, Houston, Texas.

Received 3/17/60.