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Isolation and Analysis of Hepatoma Nuclear Proteins Using Monoclonal Antibodies¹

Department of Biological Sciences, Purdue University, West Lafayette, Indiana 47907

Monoclonal antibodies were prepared to nuclear nonhistone proteins from a 2-aminoacetyl fluorine-induced transplantable rat hepatocellular carcinoma. These antibodies recognized a total of six distinct antigens as revealed by molecular weight analysis. Studies of antigen specificity with respect to various tissues, tumors, cultured cells, and oncodevelopmental stages indicated that these nuclear species could be divided into two categories. Four antigens were classified as tumor related since they were significantly enriched in tumor tissue as compared to tissues of the normal adult rat. The remaining two antigens were detected only in tumors and transformed cells; one, only in certain hepatomas. Thus, these antigens were classified as tumor specific. As an initial step toward elucidating the function of these proteins, each antigen was isolated by immunoaffinity chromatography, radioiodinated in situ, and analyzed for the ability to bind DNA. Three antigens were positive for DNA binding, and one of these was selectively released from tumor nuclei with the transcriptionally active chromatin upon digestion with micrococcal nuclease. The implications of these results for the possible functional contribution of the six tumor antigens to transformation is discussed.

¹ This work was supported by USPHS Grant 1 PO1 CA36731-O1A1 and was presented in part at the Annual Meeting of the American Society of Biological Chemists, April 1985 (60).

² Present address: Department of Chemistry, Purdue University, West Lafayette, IN 47907.

³ To whom requests for reprints should be addressed.

Received 2/29/88. Revised 6/ 1/88. Accepted 6/28/88.