Abstract

In this study, we found that rosette formation of T lymphoblastic Molt-3 cells with sheep erythrocytes is inhibited by addition of membrane glycoproteins which were solubilized from sheep erythrocyte ghosts by the lithium diiodosalicylate extraction methods. Their rosetting inhibitory activity was markedly reduced by digestion with N-glycanase, but not with O-glycanase. The inhibitory activity was also reduced by β-galactosidase digestion, while it was enhanced by desialylation. These observations indicate that nonreducing terminal galactose residues of N-linked sugar chains included in membrane glycoproteins on sheep erythrocytes are important for rosette formation with T lymphocytes.

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