Bacterial Toxins: Tools in Cell Biology and Pharmacology by Klaus Aktories

By Klaus Aktories

It is a survey of good characterised and lately found bacterial protein pollutants. top investigators of the respective pollution overview many of the molecular mechanisms of motion, starting from toxin-induced ADP-ribosylation as much as membrane perforation via pore-forming pollutants. Thy additionally describe the implications on host body structure sooner than targeting capability purposes as mobile organic and pharmacological instruments for examine and clinical functions. specified descriptions of the method comprise the engineering and use of changed and chimeric pollution for larger functionality. an excellent creation to toxin constitution and services, in addition to a necessary resource of method for researchers in molecular biology, pharmacology and experimental medication.

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In J. Biol. Chem. 253:4907-4910. Orlandi PA, Curran PK, Fishman PH (1993):Brefeldin A blocks the response of cultured cells to cholera toxin. In J. Biol. Chem. 268: 12010- 12016. Osborne JC Jr, Stanley SJ, Moss J (1985):Kinetic mechanisms of two NAD:arginine ADP-ribosyltransferases: The soluble, salt-stimulated transferase from turkey erythrocytes and choleragen, a toxin from Vibrio cholerae. In Biochemistry 24x523555240. Peterson JW, Jackson CA, Reitmeyer JC (1990):Synthesis of prostaglandins in cholera toxin-treated Chinese hamster ovary cells.

Pure CT, as iudged by isoelectric focusing, can also be obtained using Mono Q FPLC (Spangler and Westbrook, 1989). 3). , Kunkel and Robertson, 1979 and references therein). , 1994) as affinity resins; purified LT can be eluted from either matrix with galactose. Purified CTA or LTA is required for the assays described herein and can be generated and purified from CT or LT holotoxin using methods originally described for CT. , 1976) results in separation of the A subunit from B subunit monomers. , 1986).

Zhang R-G, Westbrook ML, Westbrook EM, et a/. 4 8, crystal structure of cholera toxin B subunit pentamer: Choleragenoid. In J. Mol. Biol. 251 550-562. Zolkiewska A, Okasaki IJ, Moss J (1994): Vertebrate mono-ADP-ribosyltransferases. In Mol. Cell. Biochem. 138:107-112. Cholera Toxin: Mechanism of Action and Potential Use in Vaccine Developmeni Bacterial Toxins Klaus Aktories Copyright 0 2002 WILEY-VCH Verlag GmbH & Co. KGaA Cholera Toxin and Escherichia coli Heat Ia biIe Ente rot oxin: Biochemica I Methods for Assessing Enzymatic Activities - W.

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