title: Studies on glycoproteins in the human malaria parasite Plasmodium falciparum--lectin binding properties and the possible carbohydrate-protein linkage.
abstract: 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.
authors.forename: R
authors.initials: R
authors.lastname: Ramasamy
mesh_terms: D000581:Amidohydrolases; D000818:Animals; D002241:Carbohydrates / Q000032:analysis; D005944:Glucosamine; D006023:Glycoproteins / Q000378:metabolism*; D008970:Molecular Weight; D019814:Myristic Acid; D009227:Myristic Acids; D043524:Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase; D010779:Photofluorography; D010963:Plasmodium falciparum / Q000378:metabolism*; D011952:Receptors, Concanavalin A; D011975:Receptors, Mitogen; D010738:Type C Phospholipases
chemical_list: D002241:Carbohydrates; D006023:Glycoproteins; D009227:Myristic Acids; D011952:Receptors, Concanavalin A; D011975:Receptors, Mitogen; D019814:Myristic Acid; D010738:Type C Phospholipases; D000581:Amidohydrolases; D043524:Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase; D005944:Glucosamine