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Identification and quantitation of the protein content of blood group antibody eluates prepared by the rapid acid‐stromal method
Author(s) -
Rearden A.,
Chiu P.,
Elmajian D.
Publication year - 1983
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.1537-2995.1983.23383224906.x
Subject(s) - antibody , albumin , stromal cell , microbiology and biotechnology , red blood cell , biology , transferrin , antigen , immunoelectrophoresis , blood proteins , chemistry , biochemistry , immunology , cancer research
Anti‐D sensitized red cells were converted to stroma, either by digitonin or hypotonic lysis, and eluates prepared by the modified rapid acid‐stromal method. SDS‐PAGE and both rocket‐ and crossed‐immunoelectrophoresis showed that, of the total protein content of the eluates, 11 to 25 percent was IgG, 18 to 45 percent was globin, and 34 to 71 percent was red cell membrane protein. Eluates were free of albumin, transferrin, and other non‐IgG serum proteins; they did not contain proteolytic activity, and eluates were noninhibitory to the growth of committed erythroid progenitors. The rapid acid‐stromal method produced high‐titered blood group antibody eluates free of contaminating immune or nonimmune activity which were suitable for assay of blood group antigen expression by hemopoietic stem cells and committed progenitors.