Premium
A Human Monoclonal IgM k Cold Agglutinin Recognizing Oligosaccharides with Immunodominant Sialyl Groups Preferentially at the Blood Group M‐Specific Peptide Backbone of Glycophorins: Anti‐Pr M
Author(s) -
Roelcke D.,
Dahr W.,
Kalden J.R.
Publication year - 1986
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.1423-0410.1986.tb01954.x
Subject(s) - glycophorin , cold agglutinin , cold agglutinin disease , monoclonal antibody , chemistry , antibody , peptide , hemagglutination , epitope , microbiology and biotechnology , trisaccharide , red blood cell , autoimmune hemolytic anemia , biochemistry , biology , immunology , membrane
. A k‐monotypic IgM high titer cold agglutinin reacting like anti‐Pr at low, like anti‐M at higher temperatures, is described. It recognizes tetra‐ and/or trisaccharides with immunodominant sialyl groups on glycophorins A, B, C like anti‐Pr. Its affinity to the oligosaccharides is, however, approximately 10‐fold increased when they are attached to the M‐specific peptide backbone of glycophorin A. The antibody, termed anti‐Pr M , occurred in a blood group MN patient with chronic cold agglutinin disease and caused autoimmune hemolytic anemia.