title: Egg lectin of Rana japonica and its receptor glycoprotein of Ehrlich tumor cells.
abstract: Egg lectin of Rana japonica, which specifically agglutinates transformed cells but does not agglutinate nontransformed cells and erythrocytes, has been isolated by gel filtration and successive ion-exchange chromatographies on diethylaminoethyl cellulose and carboxymethylcellulose columns and has been characterized as a homogeneous carbohydrate-free protein with a relative molecular weight of 13,500. The lectin, at a concentration of 1 microgram/0.1 ml, causes obvious cytoagglutination of various transformed and tumor cell. The receptor of the Erlich ascites tumor cells which inhibits the lectin-induced agglutination of the Ehrlich ascites tumor cells has been 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 microgram/0.1 ml, completely inhibited the cytoagglutination of the Ehrlich carcinoma cells caused by three agglutination doses (about 3 microgram/0.1 ml) of the R. japonica lectin.
mesh_terms: D000818:Animals; D001001:Anura; D001665:Binding Sites; D002286:Carcinoma, Ehrlich Tumor / Q000276:immunology*; D005260:Female; D006023:Glycoproteins / Q000276:immunology*; D037102:Lectins / Q000302:isolation & purification*; D008297:Male; D008565:Membrane Proteins / Q000276:immunology; D051379:Mice; D009363:Neoplasm Proteins / Q000276:immunology; D010063:Ovum / Q000276:immunology*; D011898:Ranidae
chemical_list: D006023:Glycoproteins; D037102:Lectins; D008565:Membrane Proteins; D009363:Neoplasm Proteins