Cell Surface Radiolabeling of the Carbohydrate Moieties of the Plasma Membrane Major Glycoprotein of AH-66 Hepatoma Ascites Cells

概要

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The major plasma memebrane glycoproteins of AH-66 cells were radiolabeled by three methods which are known to label cell surface carbohydrates. The labeled components were separated by polyacrylamide gel electrophoresis and detected by fluorography. The AH-66 cells were found to be unusual because a single major glycoprotein with an apparent molecular weight of 165000 was almost exclusively labeled by both neuraminidase-galactose oxidase-NaB^3H_4 and dilute periodate-NaB^3H_4 treatments. The major glycoprotein was not labeled by galactose oxidase-NaB^3H_4 treatment. When the major glycoprotein labeled by the neuraminidase-galactose oxidase-NaB^3H_4 procedure was solubilized with Triton X-100 and then subjected to affinity chromatography on Sepharoseconjugated Ricinus communis agglutinin II, the ^3H-labeled major glycoprotein bound to Sepharose-conjugated Ricinus communis agglutinin II lectin and was eluted with lactose. These results indicated that the major glycoprotein contained sialyl-galactosyl or sialyl-N-acetylgalactosaminyl terminal groups, which are exposed on the external surface of the plasma membranes of AH-66 cells.
公益社団法人日本薬学会の論文
1983-06-25