ANTIBODY FORMATION AND THE CODING PROBLEM,
INDIANA UNIV BLOOMINGTON DEPT OF CHEMISTRY
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The purpose of the article is to demonstrate that the template theory of antibody formation is reconcilable with the present views on coding and protein biosynthesis. The finding of the injected antigen in the microsomal fraction of spleen and liver indicates that the antigenic determinants are close to the ribosomal sites of aminoacid incorporation. It is assumed that intermolecular forces between the rigid, polar antigenic determinant and the nascent peptide chain lead to 1 the rejection of amino-acyl residues which would not allow the peptide chain to fold complementarily over the template 2 their replacement by amino-acyl residues which enable the peptide chain to form the complementary combining site of the antibody molecule. It is assumed that in this manner the amino-acid sequence dictated by the messenger-RNA is modified in that part of the antibody molecule which combines specifically with the antigenic determinant. Template action of this type may also be involved in the biosynthesis of enzymes, protein hormones or other protein molecules.