Isolation of the insulin binding alpha-one serum globulin by gelfiltration and immunosorption1

Abstract

Abstract. A radioactive alpha-one globulin, formed after infusion of labelled insulin into cats, was purified by gelfiltration and by immunosorption on immobilized antibodies against insulin. Judged by crossed immunoelectrophoresis the protein appeared to be pure. Only a fraction, about 17 per cent, of the radioactive globulin was retained by the immunosorption column. However, antibodies raised in rabbits against this protein could precipitate nearly all of the alpha-one globulin.