Abstract
The feasibility of the isolation and purification of immunoglobulin (Ig) G and albumin from human and animal blood serum by means of a uniform laboratory technique using non-chromatographic and chromatographic fractionating stages is demonstrated. The oligomerization of these proteins when stored in strong solutions of ammonium sulfate is revealed. It was ascertained that storage in sulfate suspension did not cause the fragmentation of IgG and albumin, and the degree of protein oligomerization up to 3% had no effect on the sensibility of the immunoferment assay.
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Original Russian Text © A.K. Barsukov, A.V. Barmin, A.I. Kuznetsov, O.Yu. Nesterova, S.A. Ushnurtseva, A.N. Panin, V.I. Smolenskii, V.I. Ulasov, V.L. Sviderskii, A.E. Khovanskikh, 2009, published in Prikladnaya Biokhimiya i Mikrobiologiya, 2009, Vol. 45, No. 3, pp. 378–383.
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Barsukov, A.K., Barmin, A.V., Kuznetsov, A.I. et al. The isolation of immunoglobulin G and albumin protein standards and the study of their oligomerization and antigenity during storage in saturated ammonium sulfate solution. Appl Biochem Microbiol 45, 343–348 (2009). https://doi.org/10.1134/S000368380903017X
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DOI: https://doi.org/10.1134/S000368380903017X