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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.
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