Purification of a hemorrhagic factor (LHF-I) from the venom of the bushmaster snake, Lachesis muta muta.
Hemorrhagic factor (LHF-I), was isolated from Lachesis muta muta venom by a five-step procedure. Homogeneity was demonstrated by the presence of a single band on polyacrylamide gel electrophoresis, immunoelectrophoresis and immunodiffusion. LHF-I is a glycoprotein with molecular weight of approximately 100,000 as determined by sodium dodecyl sulfate polyacrylamide-gel electrophoresis. Caseinolytic activity was associated with the hemorrhagic activity throughout the purification procedure.
D000818:Animals; D002364:Caseins; D002848:Chromatography, DEAE-Cellulose; D002850:Chromatography, Gel; D003435:Crotalid Venoms / Q000032:analysis*; D004591:Electrophoresis, Polyacrylamide Gel; D006470:Hemorrhage / Q000209:etiology*; D006868:Hydrolysis; D005779:Immunodiffusion; D051379:Mice; D008970:Molecular Weight; D010447:Peptide Hydrolases / Q000302:isolation & purification; D011817:Rabbits
D002364:Caseins; D003435:Crotalid Venoms; D010447:Peptide Hydrolases