The Ohio State University

Margaret Hanausek-Walaszek

Thomas E Webb

Dorothy E Schumm

Zbigniew Walaszek

Frank Mercurio

Raymond W Lang

A method and kit are described for detecting the presence of cancers and pre-neoplastic cells that produce an oncofetal phosphoprotein having a molecular weight of approximately 60,000 and having the capacity to increase the release of ribonucleic acid from cell nuclei. The method involves detecting the presence of auto-antibodies to this oncofetal phosphoprotein in a subject suspected of suffering from a cancer or pre-neoplastic cells which produce this cancer marker protein. The kit includes purified oncofetal phosphoprotein.

Detection of circulating antibodies to a cancer marker protein

Materials can be screened for carcinogenic properties by administering them to test animals and assaying biological tissue, preferably plasma, for the presence of a 60K cancer-associated phosphoprotein. The test is applicable to a wide range of chemically-diverse carcinogens and is not restricted to carcinogens having one particular mode of action.

Process for testing the carcinogenicity of a material or the presence of

It has previously been shown that the serum from patients suffering from a wide range of cancers contains a cancer marker protein having the ability to release RNA from cell nuclei. This cancer marker protein is purified by taking the protein fraction precipitating between 30% and 50% saturated aqueous ammonium sulfate solution, dialyzing a solution of the protein fraction against TMK buffer, chromatographing the dialyzed protein on a molecular sieve and isolating the fraction having a molecular weight of about 60,000; and removing albumin. Injection of the purified protein into rabbits, preparation of serum from blood of the rabbits and absorption of the sera with normal plasma fraction produces at antibody specific to the cancer marker protein and therefore useful in a radioimmunoassay or ELISA test for a wide variety of cancers. Monoclonal antibody preparations to the protein may be prepared by injecting the purified protein into mice, harvesting the spleen and lymph node cells, fusing these cells with mouse myeloma cells and using the resultant hybridoma cells to produce the monoclonal antibody.

Growing community of inventors

Columbus, OH, United States of America

Margaret Hanausek-Walaszek