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Ripley‐Like Anti‐Rh Associated with Red Blood Cell‐Bound IgG Aggregates
Author(s) -
Hsu T. C. S.,
LeDoux R. G.,
Sussman I. I.,
Steinberg J.,
Sawitsky A.
Publication year - 1979
Publication title -
transfusion
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.045
H-Index - 132
eISSN - 1537-2995
pISSN - 0041-1132
DOI - 10.1046/j.1537-2995.1979.19179160262.x
Subject(s) - agglutination (biology) , sephadex , chemistry , globulin , antibody , red blood cell , red cell , blood proteins , microbiology and biotechnology , immunology , chromatography , biochemistry , medicine , biology , enzyme
A commercial Rho (D) immune globulin after heating at 63 C became Ripley‐like in the Rh‐positive red blood cells coated with this heated globulin carried biologic activities similar to those of red blood cells coated with Ripley anti‐CD serum. These coated red blood cells fixed complement and were agglutinated by all 20 sera containing rheumatoid factor (RF). The RF‐Rh‐hemagglutinations were more readily inhibited by heated than by unheated human IgG. The heated globulin had no such effect on Rh‐negative red blood cells. Fractionation studies by Na2SO4 precipitation and/or Sephadex G‐200 gel filtration revealed that heat‐induced IgG aggregates in heated globulin were responsible for the biological activities. In contrast, these activities in Ripley serum were carried by IgG monomers. Another anti‐CD serum (Heyman), tested in paralledl, was found to be indistinguishable from Ripley. a pooled RF serum, after multiple adsorptions with red blood cells coated with globulin, lost its agglutination activity to red blood cells coated with Ripley or Heyman serum.