Letter | Published:

Isolation of an α2-Globulin from Human Plasma

Nature volume 192, page 1196 (23 December 1961) | Download Citation

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Abstract

WHILE examining a method for the isolation of haptoglobin by chromatography on DEAE cellulose1 we noticed that several α1- and α2-globulins were adsorbed under the experimental conditions used. One of these proteins, an α2-glycoprotein, has now been obtained at about 90 per cent purity. The protein adsorbed together with haptoglobin, cæruloplasmin, cholinesterase and some α1-globulins at pH 5.0 from human plasma diluted to a freezing point of − 0.15° is the last of these proteins to be eluted at the same pH but with increasing molarity of acetate buffer. Indeed, haptoglobin is eluted at 0.1 M acetate buffer, cæruloplasmin together with some α1-globulin at 0.2 M and the unknown protein at 0.3–0.4 M.

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References

  1. 1.

    , and , Nature, 190, 1121 (1961).

  2. 2.

    , Biochem. J., 61, 629 (1955).

  3. 3.

    , , and , Helv. Chim. Acta, 37, 886 (1954).

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Author information

Author notes

    • J. LOEB

    Chargé de recherches au Centre National de la Recherche Scientifique.

Affiliations

  1. Centre National de Transfusion Sanguine, 6 Rue Alexandre-Cabanel, Paris.

    • M. STEINBUCH
    •  & J. LOEB

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DOI

https://doi.org/10.1038/1921196a0

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