Non-hemorrhagic metalloproteinase that degrades fibrinogen. The alpha chain (FGA) is rapidly degraded, the beta chain (FGB) is degraded very slowly, while the gamma chain is left intact. Shows a prefential cleavage at X-Leu bonds. Cleaves insulin B chain at '29-His-|-Leu-30', '33-Ser-|-His-34', '38-Ala-|-Leu-39' and '40-Tyr-|-Leu-41' bonds. Binds 1 zinc ion per subunit. Its proteolytic activity is inhibited by EDTA, TPEN, 1,10-phenanthroline, and some thiol compounds, but is enhanced by alkaline earth metal ions (Mg2+, Ca2+, Sr2+, and Ba2+). Its activity is not modulated by urea (4 M). Optimum pH is 9.5. Monomer. Expressed by the venom gland. Glycosylated (Ref.1). Does not show hemorrhagic activity (Ref.1). The disintegrin domain belongs to the long disintegrin subfamily. Belongs to the venom metalloproteinase (M12B) family. P-III subfamily. P-IIIa sub-subfamily.