Chemical cross-linking studies have been carried out to investigate near neighbors to the receptor for immunoglobulin G[lgG] on U937 cells both before and after solubilization of the receptor. A cross-linked product with a molecular weight of 350.000 daltons was achieved with. DMS on intact and lysed U937 cells, DTBP on intact cells and DSS on cell lysates, with anti-FcR as the immunoprecipitation reagent. Following cross-linking of the U937 cells with DTBP and analysis by two-dimensional gel electrophoresis the p350 molecule appeared to be a p 1 70 dimer. The pl70 molecular has been related to some nonspecificity of the anti-FcR. These procedures were thus unsuccessful in identifying a neighboring molecule to the U937 cell FcR. DSS cross-linking of Fc fragments of IgG and Fab fragments of anti-FcR to the FcR on intact U937 cells was unsuccessful. Lack of success in this regard is more likely attributed to difficulties in DSS usage then to inability to cross-link close-lying molecules to the FcR. The investigations presented clarify the problems that must be overcome before successful cross-linking can be achieved between the U937 cell FcR and its neighboring molecule [s].
Library of Congress Subject Headings
Macrophages; Immunoglobulin G; Cell receptors
Department, Program, or Center
School of Chemistry and Materials Science (COS)
Malinski, Lorri Jean, "Determination of the neighboring molecule to the FC receptor on human macrophages" (1984). Thesis. Rochester Institute of Technology. Accessed from
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