New PDF release: Bacterial Toxins: Methods and Protocols

By Joseph E. Alouf (auth.), Otto Holst (eds.)

ISBN-10: 0896036049

ISBN-13: 9780896036048

The curiosity of investigators throughout a extensive spectrum of medical dis- plines has been progressively prompted by way of the sphere of bacterial toxin examine, a space that uses a wide number of organic, chemical, physicochemical, and medically orientated techniques. Researchers learning bacterial pollutants must be familiar with some of these disciplines for you to paintings successfully within the box. up to now, there was no released assortment delivering distinctive descr- tions of the thoughts and strategies wanted through researchers working around the field’sdiverse components. the current quantity Bacterial pollution: equipment and professional- cols, is meant to fill this hole. Bacterial pollutants: equipment and Protocols contains sections: one on protein pollution (15 chapters) and one on endotoxins (5 chapters). every one s- tion is brought by way of an summary article (Chapters 1 and 16). The protocols accrued signify cutting-edge concepts that every have excessive impression on destiny bacterial toxin study. All tools are defined by way of authors who've frequently been utilizing the protocol of their personal laboratories. integrated in each one bankruptcy is a short advent to the strategy being described.

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7. Measure absorbance of each fraction at 260 and 280 nm (A260 and A280) with the UV-spectrophotometer. 8. 6 or less (see Note 6). 9. Precipitate toxin pool by making 60% saturated with ammonium sulfate (see Note 7). 4. Crystallization of Type A Complex 1. 8. 2. Dialyze sample thoroughly against 3× changes of 500 mL of the same buffer (see Note 8). 34 Malizio, Goodnough, and Johnson 3. 8. 4. 9 M (see Note 9). 5. Allow crystals to form for 1–3 wk at 4°C (see Note 10). 5. Purification of Botulinum Type A Neurotoxin Recovery of neurotoxin from the complex is typically 10–13%.

1993) Quality of botulinum toxin for human treatment, in Botulinum and Tetanus Neurotoxins (DasGupta, B. ), Plenum, New York, pp. 657–659. 10. Sugiyama, H. (1980) Clostridium botulinum neurotoxin. Microbiol. Rev. 44, 419–448. 11. Schantz, E. and Scott, A. (1981) Use of crystalline type A botulinum toxin in medical research, in Biomedical Aspects of Botulism (Lewis, G. ), Academic Press, San Diego, CA, pp. 143–150. 12. Lamanna, C. McElroy, O. , and Eklund, H. W. (1946) The purification and crystallization of Clostridium botulinum type A toxin.

Nicking the A-subunit with trypsin with reduction separates the larger A1 portion (approx 28 kDa) and a smaller A2 peptide (~4 kDa). The A1 fragment contains the enzymatically active portion of the toxin molecule; however, the A2 component is required to noncovalently associate the intact A-subunit with the B pentamer (60). Whereas Stx B-subunits are not considered to be enzymatically active, serving primarily as the binding moiety for Stx holotoxin to intact cells, this may not be absolutely correct in view of work by Mangeny et al.

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Bacterial Toxins: Methods and Protocols by Joseph E. Alouf (auth.), Otto Holst (eds.)

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