PURIFICATION OF COBRA VENOM FACTOR FROM PHOSPHOLIPASE-A CONTAMINANT

  • 1 January 1976
    • journal article
    • research article
    • Vol. 31  (6) , 961-968
Abstract
It was 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 2 activities may be separated by isoelectric focusing. Cobra venom factor focuses at a pH between 5.75 and 6.75; the phospholipase is all found at a pH below 5.75. In certain test systems, particularly in vitro, and particularly where albumin concentrations are low, the contaminating phospholipase may produce effects that were attributed to complement activation.