Selective Loss of H-2 Antigenic Reactivity after Chemical Modification

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Abstract
Murine H-2 alloantigen glycoproteins were subjected to chemical modification by different modifying reagents and the effects of such modification on antigenic reactivity were evaluated. Modification of tyrosine residues using N-acetylimidazole or tetranitromethane was followed by loss of antigenic reactivity of all H-2 glycoproteins with reagents thought to be specific for amino groups, i.e., reductive alkylation and acetamidination, revealed a clear dissimilar susceptibility to inactivation. For example, for the H-2d alloantigens, specificity H-2.4 was almost totally lost and H-2.31 was almost completely retained. For the H-2b alloantigens, H-2.33 was almost completely inactivated, whereas H-2.2 and H-2.5 were affected to a much lesser degree. The reductive methylation procedure was found to change about 90% of the lysine residues to dimethylysine. The alteration of these amino groups with a direct effect on the antibody binding properties of some of the antigenic determinants on the antigen provides additional support for the view that protein structure determines antigenic H-2 reactivity.

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