Details

Autor(en) / Beteiligte

• PRENNER, C
• MACH, L
• GLÖSSL, J
• MÄRZ, L

Titel

The antigenicity of the carbohydrate moiety of an insect glycoprotein, honey-bee (Apis mellifera) venom phospholipase A2 : the role of α1,3-fucosylation of the asparagine-bound N-acetylglucosamine

Ist Teil von

• Biochemical journal, , Vol.284 (2), p.377-380

Ort / Verlag

Colchester: Portland Press

Link zum Volltext

Quelle

EZB Electronic Journals Library

Beschreibungen/Notizen

• A rabbit polyclonal antiserum raised against honey-bee (Apis mellifera) venom phospholipase A2 (PLA2) contains antibodies that react exclusively with its glycosylated variants and cross-react with plant glycoproteins. The interaction of anti-(horseradish peroxidase) antiserum with PLA2 suggests the existence of a carbohydrate determinant common to both glycoproteins. E.l.i.s.a. binding and inhibition experiments, employing glycoproteins and glycopeptides of plant and animal origin with known N-glycan structures, in combination with chemical and enzymic deglycosylation, identified alpha 1,3-fucosylation of the asparagine-bound N-acetylglucosamine as the antigenic determinant. This fucose residue is present in the N-glycan of PLA2 and is frequently found in plant glycoproteins, whereas mammalian glycoproteins lack this modification.