CARRIER-IMMOBILIZED DERIVATIZED LYSOGANGLIOSIDE GM1 IS A LIGAND FOR SPECIFIC BINDING-SITES IN VARIOUS HUMAN TUMOR-CELL TYPES AND PERIPHERAL-BLOOD LYMPHOCYTES AND MONOCYTES

Biotinylation of ganglioside-protein conjugates, derived from selective N-acylation of the sphingoid amino group of deacylated ganglioside GM1 or a ganglioside mixture, yielded probes to detect specific binding sites in fixed specimens. GM1-containing neoligandoprotein significantly bound to tumor cells in sections of 15 out of 16 cases of human lung cancer, while the probe, derived from the mixture, was ineffective under these conditions. The same graduation of staining was under identical conditions observed with these two probes on fixed human tumor cells and on peripheral blood lymphocytes and monocytes. Attempts of biochemical isolation of proteins, responsible for this binding capacity, from tumor cell extracts in the presence of the abundant endogenous ligands led to protein bands with apparent molecular weights of 44,000, 68,000 and 72,000 with yields of 0.1 - 0.24 μg/mg protein, after the detergent extracts had been passed over a resin, exposing gangliosides of the markedly less efficient mixture, to exclude binding by non-specific ionic or hydrophobic interactions. © 1990.