Abstract
Summary
A method for purification of mouse Beta 2-111 globulin is described. The purified protein is perchloric acid soluble and contains hexose, hexosamine and sialic acid. It is soluble in rivanol and binds hematin. It has a sedimentation constant of 4.3 S, indicating a molecular weight of about 65,000. It is suggested that this protein henceforth be called mouse hemopexin.
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