Several glycoproteins of the human malarial parasite Plasmodium falciparum are shown to bind to the lectins concanavalin A, wheat germ agglutinin, Ricinus communis 120 lectin and Bandeirea simplicifolia lectin. There was reduced binding of [125I]-concanavalin A to several red blood cell glycoproteins, including the anion transport protein, in parasitised cells. The carbohydrates of parasite glycoproteins are not typical N-linked oligosaccharides since the enzyme peptide: N-glyconase F fails to cleave them. In contrast, many of the parasite glycoproteins are labelled with [3H]-myristic acid consistent with a possible linkage of carbohydrate to a membrane anchoring phospholipid.