Isolation and characterization of mosquito cell membrane glycoproteins.
Autor(es): Butters T D; Hughes R C
Resumo: Plasma membranes have been purified from an established cell line, Mos 20A of Aedes aegypti, and analysed for glycoprotein and polypeptide constituents by isoelectric focusing and sodium dodecyl sulphate polyacrylamide gel electrophoresis. A major glycoprotein of molecular weight 110 000 carrying binding sites for concanavalin A and soybean agglutinin has been purified to homogeneity. Although located on the cell surface, the 110 kdalton glycoprotein is not labelled by lactoperoxidase-catalysed radioactive iodination of whole cells. Analysis indicated the presence of N-glycans, containing on average nine mannose residues, and the N-acetylglucosaminyl-beta 1, 4-N-acetylglucosamine sequence. In addition, O-glycosidically linked N-acetylgalactosamine residues are present.
Palavras-Chave: Glycoprotein isolation; Polypeptide; N-Glycan; N-Acetylgalactosamine; (Plasma membrane)
Imprenta: Biochimica et Biophysica Acta, v. 640, n. 3, p. 655-671, 1981
Identificador do objeto digital: 10.1016/0005-2736(81)90096-1
Descritores: Aedes aegypti - Cell ; Aedes aegypti - Proteins
Data de publicação: 1981
