Heterogeneous glycosylation of Musca domestica arylphorin.
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.
Marinotti
O
O
Departamento de Bioquímica, Universidade de São Paulo, Brasil.
Nunes
L R
LR
de Bianchi
A G
AG
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
D006023:Glycoproteins; D007301:Insect Hormones; D019476:Insect Proteins; C041137:storage proteins, Insecta; D003208:Concanavalin A