Three hemorrhagic factors were purified from the venom of Vipera palaestinae by gel filtration on Sephadex G-75, ammonium sulfate precipitation and DEAE-cellulose chromatography. One hemorrhagic factor is basic (HR1), one is weakly acidic and one is strongly acidic. All these factors have a similar mol. wt of about 60,000 and each of them shows one precipitin line in immunoelectrophoresis. HR1 and HR2 show both gelatinase and caseinase activity; HR3 has no detectable proteolytic activity. The basic hemorrhagic principle is a glycoprotein (positive PAS staining). Together with the weekly acidic factor it accounts for most of the hemorrhagic activity; the specific activity of each of these two components is 10 times higher than that of the crude venom.