No abstract

A new instructive type hypothesis has been formulated to account for the flow of information from an antigenic determinant to the corresponding recognition site in an antibody. It is postulated that antigen in the macrophage is broken down into determinant fragments containing about 5 aminoacyl residues. These residues attract a complementary sequence of aminoacyl groups attached to their respective s-RNA molecules, whose anticodons serve as a template for the formation of a short strand of antigenically informed RNA or cRNA. This cRNA, or its double stranded form c₂ RNA is hybridized with genomic DNA from which a cDNA results. This c₂DNA is integrated as a contiguous codon sequence into the lymphocyte gene coded for the l-chain of IgG. Synthesis of this chain and assembly of the antibody then proceeds in conventional ways and means. Hybridization of cRNA-DNA is probably the mechanism of immunologic selrecognition. This concept leads to the corolary of a symmetrical arrangement of the genetic code, including its degeneracy and redundancy. The arrangement suggests that antigen-antibody recognition is mediated by a complementary relationship between the following pairs of aminoacids: Phe-Lys, Leu-AspN, Leu-Glu, Lau-Asp, Ilu-Tyr, Meth-Tyr, Val-Glu, Val-His, Ser-Arg, Ser-Ser, Pro-Gly, Thr-Tyr, Thr-Cys and Ala-Arg.

A factor is revealed in the serum of both normal and cancer-bearing individuals which binds circulating tumor-specific antigens. This bond does not appear to be immunologic.

No abstract