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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STEINBUCH, M., LOEB, J. Isolation of an α2-Globulin from Human Plasma. Nature 192, 1196 (1961). https://doi.org/10.1038/1921196a0
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DOI: https://doi.org/10.1038/1921196a0
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