Basic Immunology by E. R. Gold and D. B. Peacock (Auth.)

By E. R. Gold and D. B. Peacock (Auth.)

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Nevertheless S, C, and E could not be distinguished serologically [28], though with the use of chicken antisera and conditions ensuring maximum precipitation A and S could be dis­ tinguished [29]. Similarly it has proved difficult or impossible to distinguish between the various insulins that differ by only one amino-acid residue, such as beef and sheep or horse and pork; though some human sera do distinguish between the first and second pairs where there is a difference of at least two amino-acids.

Separation of the chains involves rupturing a disulphide bond between residues 6 and 11 of the A chain, so here again configurational changes can be seen to alter serological specificity. We can deduce from evidence such as this that in a native protein molecule with its bent and coiled polypeptide chains the amino-acid residues that go to make up a determinant need be neither sequentially adjacent in a chain length nor indeed present in the same chain. Though it has been held that tertiary structure of a protein is determined by its primary sequence of amino-acids this may not always be so.

I, Homologous system A. 2, Homologous system B. 3, Heterologous system. Antigen A will not 'fit' antibody B. 4, Heterologous system. Antigen B will form partial 'fit' with antibody A. 2. SPECIES SPECIFICITY From the taxonomical point of view three kinds of antigen and antibody are distinguishable. A hetero-antigen is an antigen derived from a species other than that of the immunized animal. It stimulates the production of homologous hetero-antibody that may also react with antigens from animals of the same species (iso-antigens), or even with antigens from the immunized animal itself (auto-antigens).

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