EGG LECTIN OF RANA-JAPONICA AND ITS RECEPTOR GLYCOPROTEIN OF EHRLICH TUMOR-CELLS

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  • 1 January 1979
    • journal article
    • research article
    • Vol. 39  (4) , 1347-1352
Abstract
Egg lectin of R. japonica, which specifically agglutinates transformed cells but does not agglutinate nontransformed cells and erythrocytes, was isolated by gel filtration and successive ion-exchange chromatographies on DEAF cellulose and carboxymethylcellulose columns and was characterized as a homogeneous carbohydrate-free protein with a relative MW of 13,500. The lectin, at a concentration of 1 .mu.g/0.1 ml, causes obvious cytoagglutination of various transformed and tumor cells. The receptor of the Ehrlich ascites tumor cells which inhibits the lectin-induced agglutination of the Ehrlich ascites tumor cells was isolated and characterized. The receptor was solubilized from Ehrlich ascites carcinoma cells by treating a tumor cell suspension with insolubilized trypsin, and the solubilized receptor was isolated by gel filtration through Sephadex G-100, followed by ion-exchange chromatography on diethylaminoethyl cellulose. The receptor was identified as a homogeneous glycoprotein having about 25% carbohydrate. The receptor, at a concentration of 4 .mu.g/0.1 ml, completely inhibited the cytoagglutination of the Ehrlich carcinoma cells caused by 3 agglutination doses (about 3 .mu.g/0.1 ml) of the R. japonica lectin.

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