title: Purification of cobra venom factor from phospholipase A contaminant.
abstract: It has been demonstrated that cobra venom factor prepared by the usual combination of ion exchange chromatography and sephadex gel filtration is contaminated by substantial amounts of a 'heavy' phospholipase A. The two activities may be separated by isoelectric focusing. Cobra venom factor focuses at pH between 5-75 and 6-75 whereas the phospholipase is all found at pH below 7-75. In certain test systems, particularly in vitro, and particularly where albumin concentrations are low, the contaminating phospholipase may produce effects that have been attributed to complement activation.
mesh_terms: D002850:Chromatography, Gel; D002852:Chromatography, Ion Exchange; D006461:Hemolysis; D007525:Isoelectric Focusing; D010740:Phospholipases / Q000302:isolation & purification*; D012910:Snake Venoms / Q000302:isolation & purification*
chemical_list: D012910:Snake Venoms; D010740:Phospholipases