Purification and Partial Characterization of Mouse Hemopexin (Beta 2-III Globulin)

I. Witz, J. Gross

Research output: Contribution to journalArticlepeer-review


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.

Original languageEnglish
Pages (from-to)1003-1006
Number of pages4
JournalExperimental Biology and Medicine
Issue number4
StatePublished - Apr 1965
Externally publishedYes


FundersFunder number
Adolf Friedmann Endowment
Junior Kielcer Aid Society


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