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Activated human T lymphocytes display new surface glycoproteins
We have analyzed the surface glycoproteins of resting and in vitro activated human T lymphocytes by the galactose oxidase/NaB3H4 and the periodate/NaB3H4 labeling techniques. The labeled glycoproteins were separated by polyacrylamide slab gel electrophoresis and visualized by fluorography. A "new" glycoprotein with an apparent molecular weight of 130,000 (GP130) was strongly labeled on alloantigen-activated T blasts but only weakly or not at all on mitogen-stimulated T blasts and resting T lymphocytes. These results demonstrate that human T cells, as earlier found in the mouse system, express different surface molecules in relation to the particular mode of activation and stage of differentiation.
We have analyzed the surface glycoproteins of resting and in vitro activated human T lymphocytes by the galactose oxidase/NaB3H4 and the periodate/NaB3H4 labeling techniques. The labeled glycoproteins were separated by polyacrylamide slab gel electrophoresis and visualized by fluorography. A "new" glycoprotein with an apparent molecular weight of 130,000 (GP130) was strongly labeled on alloantigen-activated T blasts but only weakly or not at all on mitogen-stimulated T blasts and resting T lymphocytes. These results demonstrate that human T cells, as earlier found in the mouse system, express different surface molecules in relation to the particular mode of activation and stage of differentiation.