Selective affinity fractionation of murine cytotoxic T lymphocytes (CTL). Unique lectin specific binding of the CTL associated surface glycoprotein, T 145.

Abstract

The lectin binding characteristics of CTL-derived surface labeled glycoproteins were analyzed by affinity chromatography of the labeled glycoproteins on a panel of immobilized lectin adsorbents. Evidence was presented for the specific interaction of the CTL-associated glycoprotein T 145 with a lectin derived from Vicia villosa seeds. Conditions were described for the preparation and use of lectin affinity adsorbents for the rapid isolation of T 145 bearing CTL. T 145-Positive cells arising from a variety of T [thymus-derived] cell activations constituted the only subpopulation of cells with ability to perform cell-mediated T-cell cytotoxicity. Specific depletion of the CTL by adherence to V. villosa adsorbents was shown by their depletion in the nonbound cell fraction and correspondingly enriched recovery in the sugar eluted cell fraction. Specific affinity fractionation of CTL occurred in every strain combination tested, irrespective of the actual antigen specificity of the effector cell population.