Induces platelet activation and glycoprotein VI (GP6)-dependent platelet aggregation. Induces ectodomain cleavage of GP6 by activating endogenous platelet metalloproteinases (probably ADAM10). Has fibrinogenolytic activity against the alpha chain of fibrinogen (FGA). Recognizes distinct binding sites as convulxin, since alborhagin has minimal effect on convulxin binding to GPVI-expressing cells. Disintegrin alborhagin-C: 42 kDa fragment of alborhagin autoproteolysed that does not show platelet activation. Binds 1 zinc ion per subunit. Alborhagin-induced platelet aggregation, but not shape change, is inhibited by EDTA, suggesting that the platelet activation (shape change) is independent of divalent cation or metalloproteinase activity. Monomer. Expressed by the venom gland. Contains numerous disulfide bonds. Glycosylated. Belongs to the venom metalloproteinase (M12B) family. P-III subfamily. P-IIIb sub-subfamily.