PURIFICATION OF ANTICARDIOLIPIN AND LUPUS ANTICOAGULANT ACTIVITIES BYUSING CARDIOLIPIN IMMOBILIZED ON AGAROSE BEADS

We describe a novel method for the purification of aPL, in which pure CL is immobilized on octyl-sepharose beads by hydrophobic interaction. No lipid contamination was present in eluates, and the system could b e reutilized three times without loosing extracting capacity. Four pat ients with antiphospholipid syndrome were studied. A marked decrease i n aCL and LA activities was found in all patient plasmas after the pas sage through a CL-octyl-sepharose column. Both activities were recover ed in eluates which contained beta(2)-GP-I and IgGs. beta(2)-GP-I was also present in normal plasma eluates, which showed no aCL and slight LA activity. This method represents an improvement in the purification of aPL, and could be useful in explaining the mechanism of action of antibodies that are obtained using pure phospholipid as extracting mat rix.