Fractionation of human T lymphocytes on wheat germ agglutinin-sepharose.

T cells from human peripheral blood was purified by fractionation on columns charged with human immunoglobulin and rabbit anti-human immuno-globulin. When assayed with 125I- or fluorescein isothiocyanate-labeled wheat-germ agglutinin (WGA), a weakly binding and a strongly binding subpopulation could be distinguished. These T-cell subpopulations were fractionated on columns charged with WGA, convalently bound to Sepharose 6MB.

The interaction of nonmitogenic and mitogenic lectins with T lymphocytes: association of cellular receptor sites.

The relationship between the surface receptors on neuraminidase-treated human blood lymphocytes for the mitogenic lectins Phaseolus vulgaris leukoagglutinin (La), concanavalin A (Con A) and soy bean agglutinin (SBA) and the non-mitogenic lectin Helix pomatia A hemagglutinin (HP) was investigated. Two different techniques, co-capping with different fluorochrome-labeled lectins and cell binding-inhibition experiments with 125I-labeled lectins, were used. The results demonstrated that the nonmitogenic lectin HP and the mitogenic lectins SBA, La and Con A bind either to the same macromolecule (s) or to different but physically linked macromolecules on the surface of human T lymphocytes.

A new surface marker on T lymphocytes of human peripheral blood.

Neuraminidase treatment of human peripheral blood lymphocytes uncovers cell surface receptors that bind purified A hemagglutinin from the snail Helix pomatia. No hemagglutinin was bound to untreated lymphocytes. Binding studies with (125)I-labeled hemagglutinin suggested that the number of receptors on neuraminidase-treated lymphocytes was approximately 1.