Sialic acids are responsible for charge heterogeneity of the variant surface glycoprotein of Trypanosoma congolense.
Intact living cells of Trypanosoma congolense can be labeled by periodate/borotritide. The procedure described introduces a radioactive label nearly exclusively into the variant surface glycoprotein (VSG). The label can be removed from the VSG by either neuraminidase treatment or by mild acid hydrolysis. Using thin-layer chromatography the labeled compounds comigrated with 5-acetamido [or 5-glycolamide]3,5-dideoxygalactooctulosonic acid and 5-acetamido [or 5-glycolamide]3,5-dideoxyarabinoheptulosonic acid. These are the compounds commonly obtained after periodate borotritide treatment of glycosidically-linked neuraminic acids. It is evident from the results that sialic acids are constituents of the carbohydrate moieties of the VSG of T. congolense. Sialic acids are responsible for the charge heterogeneity of the VSG which is observed after isoelectric focusing.
D000818:Animals; D002855:Chromatography, Thin Layer; D004591:Electrophoresis, Polyacrylamide Gel; D006023:Glycoproteins / Q000032:analysis*; D007525:Isoelectric Focusing; D008565:Membrane Proteins / Q000032:analysis*; D008970:Molecular Weight; D009439:Neuraminidase / Q000378:metabolism; D012794:Sialic Acids / Q000032:analysis*; D014345:Trypanosoma / Q000032:analysis*
D006023:Glycoproteins; D008565:Membrane Proteins; D012794:Sialic Acids; D009439:Neuraminidase