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Title: Charge and size of the conversion products of serum beta-1C-globulin. Author: Lundh B, Laurell CB. Journal: Immunology; 1967 Dec; 13(6):649-55. PubMed ID: 4169023. Abstract: Using gel filtration on Sephadex G-200 combined with antigen—antibody crossed electrophoresis of the fractions, serum β1C-globulin and the conversion products present in stored native serum and stored serum to which EDTA had been added, respectively, were analysed. The conversion products in the inter-β- and γ1-zone demonstrated in EDTA serum after 1 days storage and after hydrazine treatment, respectively, could not be characterized by gel filtration, probably because of their lability. Sephadex filtration did not induce any conversion of β1C-globulin in serum. It was found that β1C- and β1A-globulin left the column in homogeneous peaks in the `7S' peak, the former slightly before the latter. The conversion product obtained in stored EDTA sera and on electrophoresis migrating in the α2-zone was found in the right extension of the macroglobulin peak. The precipitation line produced by this component was diffuse and differed distinctly from the precipitation lines of the other components. The possibility of some kind of complex is discussed.[Abstract] [Full Text] [Related] [New Search]