title: Heterogeneous glycosylation of Musca domestica arylphorin.
abstract: Two distinct fractions of Musca domestica arylphorin were isolated by affinity chromatography on Concanavalin A-Sepharose column. The results show that in the hexameric arylphorin that do not bind to the lectin there is no Concanavalin A binding subunit and in the majority of the hexamers that bind to the lectin there is only one subunit with Concanavalin A binding site. The results indicate that the carbohydrate moiety of the arylphorin is not involved in its specific uptake by the fat bodies and integument.
authors: Departamento de Bioquímica, Universidade de São Paulo, Brasil.
authors: O
authors: O
authors: Marinotti
authors: L R
authors: LR
authors: Nunes
authors: A G
authors: AG
authors: de Bianchi
mesh_terms: D000465:Algorithms; D000818:Animals; D001665:Binding Sites; D002846:Chromatography, Affinity; D003208:Concanavalin A / Q000378:metabolism; D005216:Fat Body / Q000378:metabolism; D006023:Glycoproteins; D006031:Glycosylation; D006458:Hemolymph / Q000032:analysis; D006793:Houseflies / Q000378:metabolism*; D007301:Insect Hormones / Q000378:metabolism*; D019476:Insect Proteins; D012016:Reference Values
chemical_list: D006023:Glycoproteins; D007301:Insect Hormones; D019476:Insect Proteins; C041137:storage proteins, Insecta; D003208:Concanavalin A