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Use of zinc ions for fractionation of pig γ-G-globulin and its structural subunits

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Abstract

The different behaviour of the two fractions of pig γ-G-globulin prepared by interaction with zinc ions during oxidative sulphitolysis is described. The γ-G-globulin fraction which is not precipitated by zinc ions is dissociated more readily, as seen from the finding that, unlike the other fraction, it contains practically no incompletely dissociated molecules. Fractions of the light chains, with different molecular weights, were also isolated from this fraction. A technique was elaborated for separation of the component with H antigenic specificity which is present in the light chain preparation. Detailed study of this component showed that it is probably part of the heavy chain. The origin and formation of the component is discussed.

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Authors and Affiliations

  1. Department of Immunology, Institute of Microbiology, Czechoslovak Academy of Sciences, Prague 4

    J. Rejnek, O. Kotýnek & J. Kostka

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  1. J. Rejnek
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  2. O. Kotýnek
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  3. J. Kostka
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Rejnek, J., Kotýnek, O. & Kostka, J. Use of zinc ions for fractionation of pig γ-G-globulin and its structural subunits. Folia Microbiol 12, 31–35 (1967). https://doi.org/10.1007/BF02895086

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  • DOI: https://doi.org/10.1007/BF02895086

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