Isolation of an interleukin 2-binding receptor from activated lymphocytes by high-performance immunoaffinity chromatography.

Isolation of a lymphokine-binding receptor, from activated lymphocyte membranes, can be achieved by high-performance immunoaffinity chromatography (HPIAC), using immobilized antibodies against human interleukin 2 (IL-2), as the ligand and natural IL-2 as the receptor probe. Activated lymphocytes were reacted with IL-2, sonically disrupted and their membranes solubilized, prior to passage through the HPIAC column. The IL-2 acted as an efficient receptor probe, which helped to maintain the integrity of the receptor during the isolation procedure and also acted as an attachment antigen for the immunoaffinity ligand. Recovery of the bound receptor was achieved by dissociation of the receptor-antigen-immobilized ligand complex by the action of chaotropic ions and collection of the released receptor from the column effluent during the elution phase of the separation.