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Characterization of various anti‐Pr cold agglutinins
Author(s) -
Roelcke D.,
Kreft H.
Publication year - 1984
Publication title -
transfusion
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.045
H-Index - 132
eISSN - 1537-2995
pISSN - 0041-1132
DOI - 10.1046/j.1537-2995.1984.24384225023.x
Subject(s) - cold agglutinin , medicine , immunology , antibody
Forty ‐one samples of anti‐Pr cold agglutinins (CA) were studied. The titers ranged from 4 to 32,000. As is the case with cold agglutinins of other specificities, immunoglobulin class M and k‐type light chains predominated with anti‐Pr CA. On the other hand, the few IgM lambda, IgG, and IgA found were associated preferentially with anti‐Pr specificity. All anti‐Pr CA were inhibited by human red cell membrane sialoglycoproteins. On the basis of an increased inhibition by sialoglycoproteins after periodate oxidation and carbodiimide treatment, respectively, three anti‐ Pr2 and five anti‐Pr3 were found. Among 24 anti‐Pr1 CA subclassified on the basis of agglutination with dog red cells, six were anti‐ Pr1h, 16 were anti‐ Pr1d, and two did not fit into the subclassification. Similar to the anti‐ Pr1h, ‐ Pr1d subclassification, anti‐Pr3 CA could be subclassified into anti‐ Pr3h, ‐ Pr3d. Three anti‐Pra examples were found. None of the anti‐Pr CA was inhibited by N‐acetylneuraminic acid; some (5/35) were inhibited by sialyllactose, NeuAc alpha 2–3 2–6 Gal beta 1–4Glc, in high doses (5.0‐ 20.0 mM).