The reactivity of red blood cell membrane glycophorin with “cold-reacting” antibodies

The major human erythrocyte membrane glycoprotein, glycophorin, was isolated by the method of Marchesi, using LIS (lithium 3,5-diiodosalicylate). The antigens reacting with the “cold-reacting” antibodies, anti-I, anti-i, and anti-P (Donath-Landsteiner antibody), were demonstrated to be present on th...

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Bibliographic Details
Published inClinical immunology and immunopathology Vol. 4; no. 1; pp. 1 - 8
Main Authors Lau, F.O., Rosse, W.F.
Format Journal Article
LanguageEnglish
Published United States Elsevier Inc 01.05.1975
Subjects
ABO Blood-Group System
Adsorption
Anemia, Hemolytic, Autoimmune - immunology
Animals
Antigen-Antibody Reactions
Cell Membrane - immunology
Cold Temperature
Complement Fixation Tests
Cytotoxicity Tests, Immunologic
Erythrocytes - immunology
Glycoproteins - isolation & purification
Goats - immunology
Hemoglobinuria, Paroxysmal - immunology
Humans
Immune Sera
Immunoelectrophoresis
Immunoglobulin M - isolation & purification
Iodine Radioisotopes
Isoantibodies
Rabbits - immunology
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Summary:The major human erythrocyte membrane glycoprotein, glycophorin, was isolated by the method of Marchesi, using LIS (lithium 3,5-diiodosalicylate). The antigens reacting with the “cold-reacting” antibodies, anti-I, anti-i, and anti-P (Donath-Landsteiner antibody), were demonstrated to be present on the glycophorin molecule by inhibition of antibody-induced lysis or of antibody adsorption, using radiolabeled, purified antibodies. Although these antibodies do not react with red cells at 37°C, they react with isolated glycophorin at this temperature.
ISSN:0090-1229
1090-2341
DOI:10.1016/0090-1229(75)90032-X