Surface glycoproteins from human T, B and chronic lymphatic leukemia lymphocytes isolated by 3 different lectins.

Glycoproteins from the surface of human T. B and leukemic lymphocytes were isolated and partially characterized by using three different lectins, Lens culinaris lectin (Lc), wheat germ agglutinin (WGA) and phytohemagglutinin from Phaseolus vulgaris (PHA). Cells were labelled either with I125 or 3H-fucose and lysed with detergent. Labelled components were isolated by incubation with lectins and anti-lectin antisera and immune precipitates were analysed by SDS-polyacrylamide gel electrophoresis. The results obtained show: 1) components with a molecular weight of 35,000-27,000 daltons were detected by the three lectins in both B and CLL lymphocytes but not in T lymphocytes; these components have a molecular weight similar to the Ia like antigen; 2) B and CLL lymphocytes were found to share several components of similar molecular size and specially the 35,000-27,000 daltons receptors; 3) in T lymphocytes, the 35,000-27,000 daltons components were absent, but components of low molecular weight, about 23,000, were easily detected. These data indicate that lectins bind to several identical receptors on the surface of different lymphocytes populations but also to some specific components.