نتایج جستجو برای: diphtheria toxin
تعداد نتایج: 56202 فیلتر نتایج به سال:
diphtheria is a fatal disease caused by exotoxin of corynebacterium diphtheria . this toxin consists of two chains, catalytic chain (a) and binding (b) chain. by binding chain (b), the toxin binds to its receptor on numerous body cells such as myocardial, kidney and peripheral nerve cells. after entering, catalytic chain (a) inhibits protein synthesis and finally can cause cell dea...
Background and Objective: In Indonesia, diphtheria cases caused by Corynebacterium diphtheriae are still occurring until today. One of the causes is probably the diphtheria toxin repressor (dtxR) gene which influences toxin expression. Therefore, in this study the characterization of the gene was performed to determine the mutations that affect the DtxR protein. Methods: The dtxR genes of ...
The immunodominant determinant of Pseudomonas toxin A was shown to cross-react with a normally inaccessible determinant in fragment A of diphtheria toxin. Trypsin-treated diphtheria toxin and fragment A of diphtheria toxin inhibited binding of toxin A antibody to whole toxin A, whereas whole diphtheria toxin did not inhibit this reaction. However, even at the lowest stringency no hybridization ...
Diphtheria Toxin Repressor (dtxR) Gene-Based Genetic Diversity of Corynebacterium diphtheriae Isolated in Jakarta, Indonesia, 2018–2019
The biochemical characteristics of specific receptor molecules for diphtheria toxin on the surface of two toxin-sensitive cell lines (Vero and BS-C-1) were examined. Diphtheria toxin was found to bind to a number of different proteins in Nonidet P-40 solubilized extracts of 125I-labeled cells. In contrast, permitting diphtheria toxin to bind first to labeled intact cells, which were subsequentl...
Background and Objectives: Cancer is one of the most deadly diseases in the present age and its conventional therapies have had low success. Toxin therapy of cancer is a new therapeutic approach, which has attracted the attention of pharmaceutical specialists. Diphtheria toxin consists of three functional, transducing, and binding domains, that the functional part inhibits protein synthesis and...
Ehrlich ascites tumor cells were found to be very insensitive to diphtheria toxin. We formed 37 hybrids from Ehrlich tumor cells and diphtheria toxin-sensitive human fibroblasts. The effects of diphtheria toxin on protein synthesis in those hybrids were examined. The hybrids were divided into three groups on the basis of toxin sensitivity. Group A hybrids were as sensitive to diphtheria toxin a...
The binding and uptake of fluorescently labeled diphtheria toxin by cells in culture has been examined by using epifluorescence video intensification microscopy. Rhodamine-labeled diphtheria toxin retained significant toxicity on bioassay and in cell culture and was tested for uptake by human WI-38 and mouse 3T3 fibroblasts grown in culture. When added to cells at 37 degrees C, toxin was observ...
A hybrid protein of ricin and the enzymatically active fragment A of diphtheria toxin (toxin A) has been synthesized and purified. The diphtheria toxin A fragment of the hybrid protein is shown to enter the cytosol compartment of HeLa cells, its presence assayed by the fall of intracellular elongation factor II (EF-2) and the rise of ADP-ribosylated EF-2. Hybrid entrance to HeLa cells is blocke...
We determined the diphtheria toxin phenotype of specially selected isolates of Corynebacterium ulcerans and Corynebacterium pseudotuberculosis (C. ovis). All produced proteins similar in size and immunological structure to diphtheria toxin. As with diphtheria toxin, they exhibited ADP-ribosylating activity, and their synthesis was regulated by iron.
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