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Purification and Characterization of Anti‐A Agglutinin from Euhadra callizoma amaliae
Author(s) -
Mukaida Masahiro,
Takatsu Akihiro,
Ishiyama Ikuo
Publication year - 1974
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.1423-0410.1974.tb02427.x
Subject(s) - agglutinin , melibiose , biochemistry , agglutination (biology) , concanavalin a , affinity chromatography , antigenicity , isoelectric point , hemagglutination , microbiology and biotechnology , albumin , chemistry , raffinose , lectin , biology , antibody , enzyme , maltose , in vitro , immunology , sucrose
. Snail agglutinin (anti‐AEc, anti‐A 1 of cold agglutinin type) from the albumin gland of Euhadra callizona amaliae was purified by affinity chromatography (meconium‐A aminoethyl cellulose). Its physicochemicl properties are as follows: S 20, w : 5.3S. Isoelectric point: pH 3.6. Molecular weight: 8.9 × 10 4 . Hexose content: 5.1%. The amino acid composition is that of an acidic protein. The agglutination is inhibited by GalNAc, GNAc, raffinose, and melibiose at low concentration. It does not agglutinate B‐ and O‐RDE‐treated human red cells. Some blood group A‐active substances (secretor A saliva and hog gastric mucin A + H) have low potency to inhibit the agglutination. Anti‐ABC has no ability to release the cell‐fixed anti‐Eorssman haemolysin and the cell‐fixed blood group A‐decomposing enzyme. The significance of the antigen distribution on the limited area of the erythrocyte and protein surface is also discussed. Precipitin reaction of this agglutinin with various blood group‐active substances has shown that anti‐AEc is directed to a narrow‐range spectrum of determining antigenicity.