By Klaus Aktories
It is a survey of good characterised and lately stumbled on bacterial protein pollution. major investigators of the respective pollutants evaluation a number of the molecular mechanisms of motion, starting from toxin-induced ADP-ribosylation as much as membrane perforation by means of pore-forming pollutants. Thy additionally describe the implications on host body structure prior to targeting capability functions as phone organic and pharmacological instruments for examine and scientific purposes. distinctive descriptions of the method comprise the engineering and use of transformed and chimeric pollution for larger functionality. a great advent to toxin constitution and capabilities, in addition to a invaluable resource of method for researchers in molecular biology, pharmacology and experimental medication.
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Additional resources for Bacterial Toxins: Tools in Cell Biology and Pharmacology
At 30°C. NAD glycohydrolase 2. After the incubation, duplicate samples from each tube are transferred to AG 1-X2 columns and handled further as described in Assay 2. Table 4. 025 pCi 1 Yg 1 Pg ’ Rather than adding individual components to each tube, phosphate buffer and lipid can be added as a mixture, followed by a mixture (of intermediate volume) that contains all components except ARF and activated toxin, and then by successive addition of each of the other components. Addition of components in the order described prevents the precipitation of phosphate and magnesium.
Field M (1971): Intestinal secretion: Effect of cyclic AMP and its role in cholera. In N. Engl. J. Med. 284:1137-1144. Finkelstein RA, LoSpalluto JJ (1969): Pathogenesis of experimental cholera: Preparation and isolation of choleragen and choleragenoid. In J. Exp. Med. 130:185-202. Fishrnan PH (1982): Role of membrane gangliosides in the binding and action of bacterial toxins. In J. Membr. Biol. 69:85-97. Fontana MR, Manetti R, Giannelli V, et a/. (1995): Construction of nontoxic derivatives of cholera toxin and characterization of the immunological response against the A subunit.
It is possible that the toxin was not properly activated, and a new sample of toxin should be activated, using freshly prepared DTT. It is possible that the concentration of NAD in the assay was too low and was hydrolyzed. Because NAD in solution is susceptible to hydrolysis, it should be stored in small portions at -20°C and the stock supply replaced regularly. Mutant toxins may, in fact, be inactive and it is suggested that Assays 3 and 4 be used to confirm or negate this possibility. CT activity may also be affected by salt and/or protein concentrations in the assay.