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- W2000405469 abstract "Lectins covalently bound to Sepharose 4B were employed, in the presence of 1 % sodium deoxycholate, to purify glycoproteins from isolated plasma membranes of normal and transformed fibroblasts. Lectins used in this study were isolated from Lens culinaris (LcH) and Ricinus communis (RCAI) and were specific for d-glucose and d-mannose (LcH) and d-galactose (RCAI), respectively. Approx. 5% of the total plasma membrane protein applied to the LcH-containing column bound and was eluted specifically, whereas approx. 3% was bound and specifically eluted from the RCAI column. A comparison of bound glycoproteins from normal and transformed cells by SDS polyacrylamide gel electrophoresis demonstrated that a glycoprotein of 85 000 D was present in substantially greater amounts in normal cell isolates. Another glycoprotein of 130000 D was found in higher concentration in transformed cell plasma membranes. The 85 000 D protein was shown to be a subunit of a serum protein of greater than 300 000 D which has a specific affinity for the normal but not transformed cell surface. These results are discussed in relation to the differential agglutinability of normal and transformed cells by plant lectins." @default.
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- W2000405469 date "1977-10-01" @default.
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- W2000405469 title "Isolation and partial characterization of plasma membrane glycoproteins from normal and transformed mammalian cells employing plant lectin affinity chromatography*1" @default.
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- W2000405469 doi "https://doi.org/10.1016/0014-4827(77)90048-9" @default.
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