The inhibition of thromboplastin by apolipoprotein-B and the effect of various associated lipids.

Human apolipoprotein B was purified by barium sulphate adsorption, subsequent delipidation and gel filtration. The protein was then reconstituted in soya bean lecithin and its inhibitory effect towards thromboplastin was assayed by incubation with rabbit brain thromboplastin. The use of an antibody against human apolipoprotein B diminished this inhibition. The level of inhibition of thromboplastin by the reconstituted apolipoprotein was found to be dependent on the concentration of the phospholipids with which it was reconstituted, reaching a maximum inhibition at a lipid: protein ratio of 1:1 (w/w). However, higher phospholipid concentrations or inclusion of cholesterol esters or triglycerides diminished and at certain concentrations reversed the inhibitory effect of the apolipoprotein. These results point towards apolipoprotein B as an inhibitor whose activity towards thromboplastin could be dependent on the complexes it forms with the surrounding lipids.