DETECTION OF THE GANGLIOSIDE N-GLYCOLYL-NEURAMINYL-LACTOSYL-CERAMIDE BY BIOTINYLATED ESCHERICHIA-COLI K99 LECTIN

K99 lectin from Escherichia coli was purified and biotinylated via its carboxyl groups using biocytin hydrazide and a water soluble carbodii mide. Biotinylation of two out of the nine carboxyl groups was suffici ent to permit detection of the lectin by avidin and did not cause any loss of the haemagglutinating activity. It was demonstrated that the b iotinylated K99 lectin retained other important properties of native K 99 and that it will probably become a very sensitive detecting reagent . Indeed, it was able to bind to HeLa cells, as to do intact bacteria carrying K99 fimbriae, and also to recognize N-glycolyl-neuraminyl-lac tosyl-ceramide in an overlay binding assay.