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[Cancer Research 38, 4440-4444, December 1, 1978]
© 1978 American Association for Cancer Research

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Isolation and Partial Characterization of a 67Ga-binding Glycoprotein from Morris 5123C Rat Hepatoma1

DeSales Lawless2, David H. Brown3, Karl F. Hubner, Shirley P. Colyer, James E. Carlton and Raymond L. Hayes

Medical and Health Sciences Division, Oak Ridge Associated Universities,4 Oak Ridge, Tennessee 37830

A glycoprotein, particularly high in tumors, has been extracted from Morris 5123C rat hepatomas and purified. The compound constitutes a major binding component for 67Ga in this hepatoma. It has a molecular weight of approximately 45,000. Its molecular weight was determined by sodium dodecyl sulfate:polyacrylamide gel electrophoresis and by Sephadex G-200 superfine gel filtration. The steps involved in its extraction and purification include ultrafiltration, gel filtration through Sephadex G-200 superfine, ion-exchange chromatography on diethylaminoethyl Sephadex A-50, and hydroxylapatite chromatography. The homogeneity of the compound was established by gel electrophoresis. The NH2-terminal residue, the percentage of nitrogen, the nonamino carbohydrate content, and the amino acid composition are reported.

1 This work was supported by NIH, Department of Health, Education and Welfare, Grant CA-11858.

2 Present address: Fordham University, New York, N. Y.

3 To whom requests for reprints should be addressed.

4 Operated for the United States Department of Energy under Contract EY-76-C-05-0033.

Received 6/ 9/78. Accepted 9/ 6/78.







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Copyright © 1978 by the American Association for Cancer Research.