Abstract

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

Publication Date

1984

Document Type

Thesis

Department, Program, or Center

School of Chemistry and Materials Science (COS)

Advisor

Names Illegible

Comments

Note: imported from RIT’s Digital Media Library running on DSpace to RIT Scholar Works. Physical copy available through RIT's The Wallace Library at: QR186.8.G2 M3 1984

Campus

RIT – Main Campus

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