Twenty-seven different immunoglobulins prepared from sera and urine of BALB/c mice with plasma cell tumors were tested with a variety of mouse allotype antisera reacting with immunoglobulins of normal BALB/c mice. None of the antisera obtained from 15 different donor-recipient combinations reacted in Ouchterlony precipitin tests with the one γM- and three γA-immunoglobulins nor with the ten λ and two κ light polypeptide chains from mice with plasma cell tumors. Several of the antisera gave weak precipitin reactions near the antigen well with some of the five immunoglobulins designated γF; these reactions were interpreted as the probable result of contamination with small amounts of immunoglobulins from normal plasma cells.

The antisera distinguished between two classes of γG-immunoglobulins designated γG-Be1 and γG-Be2. Some antisera gave dense precipitin bands with the three tumor-derived γG-Be2 immunoglobulins as well as the corresponding γG-Be2 immunoglobulin in normal serum but not with the three tumor-derived γG-Be1 immunoglobulins. Similarly, some antisera gave dense precipitin bands with the three tumor-derived γG-Be1 immunoglobulins as well as the corresponding γG-Be1 immunoglobulin in normal serum but not with the three tumor-derived γG-Be2 immunoglobulins. The allotypic specificities which distinguish between γG-Be1 and γG-Be2 (designated a1′ and a1") were found to be associated with the papain Fc-fragment, a part of the heavy polypeptide chain.

Antisera specific for γG-Be1 and γG-Be2 (anti-a1′ and anti-a1″) were used to test F2 progeny for independent assortment or linkage. The a1′ and a1″ allotypic specificities were either both present or both absent in the same F2 progeny indicating close linkage in their genetic control.

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