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Immunological Identification of Blood Group P k Antigen on Normal Human Erythrocytes and Isolation of Anti‐P k with Different Affinity
Author(s) -
Naiki Masaharu,
Kato Michimasa
Publication year - 1979
Publication title -
vox sanguinis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.68
H-Index - 83
eISSN - 1423-0410
pISSN - 0042-9007
DOI - 10.1111/j.1423-0410.1979.tb02265.x
Subject(s) - antigen , antibody , complement fixation test , hemagglutination , glycolipid , chemistry , microbiology and biotechnology , absorption (acoustics) , reagent , abo blood group system , stereochemistry , biochemistry , immunology , biology , serology , physics , acoustics
. The P 1 and P k blood group glycolipid antigens have the common terminal disaccharide, Gal(α, 1–4)Gal, but previous studies indicated that anti‐P 1 from P 2 individuals does not cross‐react with P k antigen. In this paper, the specificities of anti‐P 1 and anti‐P k were analyzed carefully by complement fixation and hemagglutination techniques and the following results were obtained: (1) Anti‐P 1 from P 2 serum was not absorbed with the P k glycolipid (CTH), but this antigen absorbed all anti‐P 1 and anti‐P k (anti‐P 1 P k ) antibodies from the sera of four p individuals. Most of the anti‐P 1 P k antibodies were IgG, but the anti‐P 1 from the P 2 individual was IgM. (2) The P k antigen on normal P 2 erythrocytes was not ‘cryptic’. It was reactive with p serum from which the anti‐P antibodies were removed by absorption with the P glycolipid (globoside). This was not appreciated previously because, in order to make anti‐P k reagents, p sera (anti‐P 1 PP k ) were absorbed with P 1 cells which contain CTH. (3) The anti‐P 1 P k antibodies in p sera were separated by partial absorption with P 1 erythrocytes and elution from the absorbing cells, into two fractions that differ markedly in their affinity for α‐methyl‐ D ‐galactoside and the oligosaccharides prepared from CTH.