The specificity anti-Gd of human cold autoagglutinins is characterized using
untreated and enzyme-treated human red blood cells. Gd determinants of human RBC are
resistant to proteases, but are inactivated by neuraminidase (RDE). In contrast, I/i determinants
are not inactivated by proteases or RDE, while Pr(1-3) determinants are inactivated by proteases
and RDE, and Pr(a) determinants are resistant to RDE, but are inactivated by proteases.
A monoclonal IgM (y) anti-Pr cold agglutinin occurring after a
rubella infection is shown to have the ‘new’ anti-Pr subspecificity anti-Pr3. Pr3
determinants are found on cat and sheep erythrocytes which lack Prt and Pr2
determinants. By carbodiimide treatment of human erythrocyte glycoproteins,
which causes intramolecular coupling of IV-acetylneuraminic acid carboxyl groups
and nucleophilic centers of the glycoprotein backbone, Pr3 antigen activity is
strongly increased, while Pr, and Pr2 determinants are inactivated.
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