Complete amino acid sequence of variable domains from two monoclonal human anti-gamma globulins of the Wa cross-idiotypic group: suggestion that the J segments are involved in the structural correlate of the idiotype.

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Abstract
The complete amino acid sequences of the variable regions of 2 human IgM anti-.gamma.-globulins are reported. The 2 proteins, Sie and Wol, share idiotypic determinants that are distinct from those shared by the 2 previously sequenced IgM anti-.gamma.-globulins, Lay and Pom. In contrast to Lay and Pom, Sie and Wol have very little homology in the complementarity-determining hypervariable regions of either their L or H polypeptide chains. However, there are only 2 amino acid differences in the framework portions of the L chains and the J segments of both chains are homologous. The predominant idiotypic determinant in this cross-idiotypic system may be different than in the Po group and may be either related to their L chain framework structures or to the amino acid sequence in the J segments of these molecules.