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Apolipoprotein B, the core polypeptide of human serum low-density lipoprotein, retains its native association state (500 000 g/complex), as well as its native conformation as judged by circular dichroism, when all lipid has been replaced by a nonionic detergent. Protein solubilized in this detergent should therefore be well suited for lipid binding studies. The native association state is also preserved when lipid is replaced by ionic detergents, but in this case the protein undergoes a conformational change, which can be reversed if the ionic detergent is replaced by nonionic detergent. The constancy of the state of association of the B polypeptide in a variety of amphiphilic environments contrasts with what has been observed with polypeptides from high-density lipoproteins which exist in different states of association under different conditions.

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Inhibitors to coagulation factors are among the most difficult problems in the management of coagulation disorders. Most presently available therapy does not assure hemostasis. An extracorporeal immunoadsorption system, which selectively binds IgG, was used to lower inhibitor levels in eight patients on 10 occasions. In this system, separated plasma is delivered to two staphylococcal protein A-Sepharose columns, which are coupled to an elution monitor. Columns are eluted sequentially and regenerated to maximize IgG removal. Successful removal of the inhibitor was accomplished in all six hemophiliacs on seven occasions, as well as in a patient with acquired von Willebrand disease. All patients whose inhibitors were lowered to less than 10 Bethesda units achieved measurable factor levels when factor concentrate replacement was given. Immunoadsorption facilitates efficient removal of inhibitors, which allows factor replacement therapy.