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.
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