Folia Microbiologica

, Volume 12, Issue 1, pp 31–35 | Cite as

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

  • J. Rejnek
  • O. Kotýnek
  • J. Kostka


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.


Light Chain Papain Ammonium Carbonate Sodium Sulphite Immunoelectrophoretic Analysis 
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Copyright information

© Institute of Microbiology, Academy of Sciences of the Czech Republic 1967

Authors and Affiliations

  • J. Rejnek
    • 1
  • O. Kotýnek
    • 1
  • J. Kostka
    • 1
  1. 1.Department of Immunology, Institute of MicrobiologyCzechoslovak Academy of SciencesPrague 4

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