نتایج جستجو برای: diphtheria toxin

تعداد نتایج: 56202  

Journal: :Proceedings of the National Academy of Sciences of the United States of America 1978
R K Draper D Chin M I Simon

The inhibition of protein synthesis in Chinese hamster V79 cells by diphtheria toxin is antagonized by the lectins concanavalin A, succinylated concanavalin A, and wheat germ agglutinin but not by Proteus vulgaris phytohemagglutinin or abrus agglutinin. The effects of concanavalin A and wheat germ agglutinin are reversed by methyl alpha-mannoside and N-acetylglucosamine, respectively. The inhib...

Journal: :Nippon Saikingaku Zasshi 1987

Journal: :The Journal of Cell Biology 1984
K Sandvig A Sundan S Olsnes

Inhibition of protein synthesis in Vero cells was measured at different periods of time after treatment with diphtheria toxin and the related plant toxin modeccin. Diphtheria toxin acted much more rapidly than modeccin. Cells were protected against both toxins with antiserum as well as with agents like NH4Cl, procaine, and the ionophores monensin, FCCP, and CCCP, which increase the pH of intrac...

Journal: :Proceedings of the National Academy of Sciences of the United States of America 1989
J M Rolf H M Gaudin S M Tirrell A B MacDonald L Eidels

An anti-idiotypic serum prepared against the combining site (idiotype) of specific anti-diphtheria toxoid antibodies was characterized with respect to its interaction with highly diphtheria toxin-sensitive Vero cells. Although the anti-idiotypic serum protected Vero cells against the cytotoxic action of diphtheria toxin, it did not prevent the binding of 125I-labeled diphtheria toxin to the cel...

Journal: :Journal of bacteriology 1938
M D Eaton A Gronau

Diphtheria toxin has been identified as a typical heat-coagulable protein (Eaton 1936 a, 1937; Pappenheimer 1937). If other toxins have chemical properties similar to diphtheria toxin, they might be isolated by similar methods. Using a gelatin hydrolysate medium, Pappenheimer and Johnson (1936, 1937) have produced diphtheria toxin which may be obtained in a relatively pure state by simple fract...

2003
C. W. SPEARING

WARREN, LEONARD (National Institute of Arthritis and Metabolic Diseases, Bethesda, Md.) AND C. W. SPEARING. Sialidase (neuraminidase) of Corynebacterium diphtheriae. J. Bacteriol. 86:950-955. 1963.-The characteristics of a sialidase produced by Corynebacterium diphtheriae were studied. The enzyme was partially purified from preparations of diphtheria toxin on a column of Sephadex G-75. By this ...

Journal: :Proceedings of the National Academy of Sciences of the United States of America 1974
B H Iglewski M B Rittenberg

Purified diphtheria toxin is shown to inhibit protein synthesis in Ehrlich-Lettré ascites carcinoma cells in vitro. Protein synthesis in Ehrlich-Lettré cells is at least 10,000 times more sensitive to toxin than protein synthesis in normal mouse spleen or thymus cells. This sensitivity correlates with the observation that Ehrlich-Lettré tumors regress in mice injected with diphtheria toxin but ...

Journal: :Journal of cell science 1999
G Skretting M L Torgersen B van Deurs K Sandvig

We have here used diphtheria toxin as a tool to investigate the type of endocytosis used by a glycosylphosphatidylinositol-linked molecule, a glycosylphosphatidylinositol-linked version of the diphtheria toxin receptor that is able to mediate intoxication. The receptor is expressed in HeLa cells where clathrin-dependent endocytosis can be blocked by overexpression of mutant dynamin. Diphtheria ...

Journal: :Vaccine 2004
Niclas Rydell Ingvar Sjöholm

Oral vaccination offers the advantage of eliciting both a mucosal and a systemic immune response. This study investigated the use of polyacryl starch microparticles as adjuvant for oral vaccination against diphtheria. Diphtheria toxin or cross-reacting material (CRM197) were covalently conjugated to the microparticles and fed to mice by oral gavage. Investigation of formaldehyde treatment as a ...

Journal: :The Journal of Experimental Medicine 2003
Jules Freund

1. Collodion particles adsorb diphtheria or tetanus or botulinus toxins. These toxins are retained on the particles when washed but are at least in part released in the animal. 2. The adsorbed toxins are neutralized by adsorption of the corresponding antitoxins but are unaffected by other serums. 3. When collodion particles are treated first with tetanus antitoxin, then with diphtheria toxin, t...

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