Diphtheria toxin receptor.
نویسندگان
چکیده
منابع مشابه
Hypersensitivity to diphtheria toxin by mouse cells expressing both diphtheria toxin receptor and CD9 antigen.
DTS-II is a highly diphtheria toxin (DT)-sensitive cell line previously isolated by transfection of wild-type DT-resistant mouse L-M(TK-) cells with the cDNA encoding a monkey Vero cell DT receptor. DTS-II cells are as toxin-sensitive as Vero cells, have approximately 3-fold more receptors than Vero cells, and have approximately 10-fold lower affinity for DT than Vero cells. We now cotransfecte...
متن کاملIdentification of diphtheria toxin receptor and a nonproteinous diphtheria toxin-binding molecule in Vero cell membrane
Two substances possessing the ability to bind to diphtheria toxin (DT) were found to be present in a membrane fraction from DT-sensitive Vero cells. One of these substances was found on the basis of its ability to bind DT and inhibit its cytotoxic effect. This inhibitory substance competitively inhibited the binding of DT to Vero cells. However this inhibitor could not bind to CRM197, the produ...
متن کاملPurification of diphtheria toxin receptor from Vero cells.
Diphtheria toxin receptor has been solubilized from Vero cell membranes with octyl beta-D-glucoside. CRM197, the product of a mutated diphtheria toxin gene, was used for the identification of the receptor. The binding activity of the solubilized receptor was assayed by precipitating the receptor with acetone in the presence of phospholipids and carrier proteins. The solubilized receptor was pur...
متن کاملDiphtheria Toxin In
Recent studies have demonstrated that diphtheria toxin is an enzyme of unusual type. Small amounts of the toxin, added to nicotinamide adenine dinucleotide (NAD)-containing mammalian cell extracts, block peptide-bond formation by catalyzing inactivation of the translocating enzyme, aminoacyltransferase 2 (T2) (1-3). This highly specific reaction involves the splitting of NAD with liberation of ...
متن کاملThe role of the diphtheria toxin receptor in cytosol translocation.
The role of the receptor in the transport of diphtheria toxin (DT) to the cytosol was examined. A point-mutant form of DT, CRM 107 (CRM represents cross-reacting material), that has an 8,000-fold lower affinity for the DT receptor than native toxin was conjugated to transferrin and monoclonal antibodies specific for the cell-surface receptors T3 and Thy1. Conjugating the binding site-inactivate...
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ژورنال
عنوان ژورنال: Nippon Saikingaku Zasshi
سال: 1993
ISSN: 1882-4110,0021-4930
DOI: 10.3412/jsb.48.685