Neuraminidase “Unmasking” and Failure of Trypsin to “Unmask” β- D -Galactose- Like Sites on Erythrocyte, Lymphoma, and Normal and Virus-Transformed Fibroblast Cell Membranes 2

作者：Garth L. Nicolson · 发表于：JNCI Journal of the National Cancer Institute · 年份：1973 · DOI：10.1093/jnci/50.6.1443 · 被引用次数：92 · 研究领域：Toxoplasma gondii Research Studies、Glycosylation and Glycoproteins Research、Polyamine Metabolism and Applications

Treatment of human erythrocytes,mouse lymphoma, and normal and simian virus 40 (SY40)transformed 3T3 fibroblast cells with Vibrio cholerae or Clostridium perfringens neuraminidase generally increased their agglutinability with Ricinus communis agglutinin. Saturation binding of 125I-labeled R. communis agglutinin at 4° C revealed that the neuraminidase-treated cells specifically bound 1.5–3 times as many agglutinin moleculesas did untreated cells. Brief trypsinization of these cells also resulted in increased agglutinability with R. communis agglutinin, but the number of 125I-labeled agglutinin molecules bound after trypsin treatment was the same or less than the number bound to untreated cells. Normal 3T3 cells were compared to SV40-transformed 3T3 cells; confluent 3T3 cells bound the same number of R. communis agglutinin molecules as did the transformed SY3T3, though the SV3T3 cells were more agglutinable. The results were discussed in relation to factors which control cell agglutination.