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Cell surface radiolabeling of the carbohydrate moieties of the plasma membrane major glycoprotein of AH-66 hepatoma ascites cells.

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-NaB3H4 and dilute periodate-NaB3H4 treatments. The major glycoprotein was not labeled by galactose oxidase-NaB3H4 treatment. When the major glycoprotein labeled by the neuraminidase-galactose oxidase-NaB3H4 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.