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Specificity of Limulus polyphemus Agglutinins for Erythrocyte Receptor Sites Common to M and N Antigenic Determinants
Author(s) -
Cohen E.,
Roberts S. C.,
Nordling S.,
Uhlenbruck G.
Publication year - 1972
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.1423-0410.1972.tb03464.x
Subject(s) - limulus , horseshoe crab , agglutination (biology) , antigen , antibody , agglutinin , biology , microbiology and biotechnology , receptor , chemistry , immunology , biochemistry , lectin , paleontology
. The ability of human erythrocytes to absorb Limulus polyphemus (Horseshoe Crab) agglutinins was demonstrated to be significantly reduced by prior coating of erythrocytes with rabbit anti‐M or anti‐N antibodies. Inhibition of Limulus agglutinin absorption could also be demonstrated using heterozygous MN cells coated with either anti‐M or anti‐N. Normal rabbit serum did not reduce the absorption of Limulus agglutinins. However, human MN mucoid substances, extracted from stromata, inhibited agglutination of human erythrocytes by Limulus agglutinins, as well as rabbit anti‐M and anti‐N. These experiments suggest that the N‐acetyl‐neuraminyl (NANA) receptor site for Limulus agglutinins, designated anti‐NANA I,P , is common to both M and N antigenic determinants. The NANA‐specific site cannot, therefore, be used to differentiate N from M antigens.