Abstract
Two immunoelectrophoretically defined, heretofore unidentified β1-globulins of human serum, provisionally designated β1C- and β1A-globulin, were isolated by means of preparative electrophoresis and chromatography on anion exchange cellulose. The sedimentation coefficient S0 20, w of β1C-globulin was shown to be 9.5 S, and that of β1A-globulin, 6.9 S. Both proteins were found to contain similar amounts of carbohydrate, to be devoid of lipids, and to possess the solubility characteristics of euglobulins. In the Ouchterlony double diffusion test they gave the reaction of partial identity, which revealed β1A-globulin to be anti-genically deficient as compared to β1C-globulin. β1A-globulin could not be detected in fresh sera and β1C-globulin was absent from aged sera. Highly purified β1C-globulin stored at 1°C. was converted to β1A-globulin within 4 to 6 weeks, and at 37°C. was converted within 6 days. The likelihood of a dimer-monomer relationship between these two proteins was discussed.
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Selected References
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