Preliminary characterization of a glycoprotein having Fc receptor properties extracted from a T cell lymphoma (L-5178-Y).

After incorporation of 14C-labeled amino acids and/or of [3H]fucose during in vitro culture of the Thy-1.1-bearing, Fc receptor-positive T lymphoma, L-5187-Y, attempts were made to purify the Fc binding structure(s). Following solubilization of a crude membrane pellet using sodium deoxycholate, the 110 000 x g supernatant was filtered on Sephadex G-200, and the fractions containing IgG-binding material were further purified by affinity chromatography (on IgG Sepharose 4B.) Sodium dodecyl sulfate polyacrylamide gel electrophoretic analysis of the final Fc-binding product showed an apparent molecular weight of 110 000 daltons. On subsequent reduction with 2-mercaptoethanol, five bands (mol. wts. 56 000, 36, 000, 25 000, 18 000 and 15 000) were observed, the latter two being probably degradation products. These results are in accord with some of the published data concerning B cell Fc receptors.