The major sialoglycoprotein of human T-lymphocytes.
Human, peripheral-blood T-lymphocytes and human, T-lymphoblastoid cells of a MOLT 4B cell-line were surface-labeled by lactoperoxidase-catalyzed iodination, periodate and sodium borotritide, and galactose oxidase and sodium borotritide, and analyzed by dodecyl sodium sulfate-polyacrylamide gel-electrophoresis. Both types of cells were found to show a major, cell-surface sialoglycoprotein with an apparent mol. wt. of 95,000. After neuraminidase treatment, this glycoprotein showed a higher mol. wt. of 120,000. The major sialoglycoprotein of both types of cells bound to wheat-germ agglutinin and concanavalin A and, after neuraminidase treatment, to Arachis hypogaea agglutinin. The glycopeptides obtained from these glycoproteins by Pronase digestion gave similar elution-profiles on Sephadex G-50 gel filtration. These results suggest that the major sialoglycoprotein of normal T cells and that of MOLT 4B cells are very similar, if not identical.
D002460:Cell Line; D002462:Cell Membrane / Q000032:analysis; D006020:Glycopeptides / Q000032:analysis; D006801:Humans; D037102:Lectins; D008565:Membrane Proteins / Q000032:analysis*; D008970:Molecular Weight; D009439:Neuraminidase; D012795:Sialoglycoproteins / Q000032:analysis*; D013601:T-Lymphocytes / Q000032:analysis*
D006020:Glycopeptides; D037102:Lectins; D008565:Membrane Proteins; D012795:Sialoglycoproteins; D009439:Neuraminidase