Use of zinc ions for fractionation of pig γ-G-globulin and its structural subunits
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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.
KeywordsLight Chain Papain Ammonium Carbonate Sodium Sulphite Immunoelectrophoretic Analysis
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- Franěk, F., Zikán, J.:United cleavage of disulphide bonds of pig γ-globulin by S-sulfonation. Collection Czech. chem. Commun. 29: 1401, 1964.Google Scholar
- Nussenzweig, V., Benacerraf, B.:Presence of identical antigenic determinants in the Fd fragments of γ 1 and γ 2 guinea pig immunoglobulins. Information Exchange Group 5: 45, 1965.Google Scholar
- Škvařil, F., Rejnek, J.:Our experience with micromodification of immunoelectrophoresis. Čs. epidemiol. mikrobiol. imunol. 7: 414, 1958.Google Scholar