Seafood and freshwater toxins: pharmacology, physiology, and by Luis M. Botana

By Luis M. Botana

The previous couple of years have led to many adjustments within the box of marine and freshwater pollutants, with advances in analytical expertise and the conclusion that those pollution are a world factor. delivering a whole reference consultant, Seafood and Freshwater pollutants: Pharmacology, body structure, and Detection, 3rd Edition addresses all features of the social and medical effect of phytotoxins, from laws and tracking to new drug improvement. masking many new issues, the e-book examines 3 major features: tracking of poisons; chemical, mechanistic, and toxicological variety; and detection technologies.

New to this edition:

  • 35 new chapters and five up to date chapters
  • A specialize in state of the art methodology
  • Coverage of latest applied sciences to domesticate algae and to spot, isolate, and quantify toxins
  • Regulatory changes
  • Climate swap evidence
  • Expanded info on toxicology

Part I of the e-book contains an outline and reports common matters regarding toxin detection, ecology, and variety, and results of weather switch. half II covers affects of poisons relating to epidemiology, toxicology, economics, and surveillance. half III explores on hand detection applied sciences, resembling useful assays, biosensors, mass spectrometry, nanotechnology, and extra. moreover, typical reference fabrics for pollution are mentioned. components IV to VI supply distinctive descriptions of toxin chemical range, organic resources, and modes of motion. half VII addresses using pollution as beginning issues for healing medicinal drugs for melanoma, neurological issues, and for novel antibiotics.

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Extra resources for Seafood and freshwater toxins: pharmacology, physiology, and detection

Sample text

1–10 nM, depending on the congener). Both the cyanobacterial cyclic peptide toxins and the dinoflagellatederived protein phosphatase inhibitor, okadaic acid, bind to the catalytic subunit of the protein phosphatases. X-ray crystal structures (79), molecular modeling (80), and mutational analyses (81) indicate that all three toxin classes bind to the same site. However, unlike the other toxin classes, the microcystins form covalent adducts with Cys273 in the enzyme subsequent to binding (126). Figure 14 Cyclic peptide toxins from cyanobacteria.

A Morohashi, M Satake, K Murata, H Naoki, HF Kaspar, T Yasumoto. Brevetoxin B3, a new brevetoxin analog isolated from the greenshell mussel Perna canaliculus involved in neurotoxic shellfish poisoning in New Zealand. Tetrahedron Lett 36:8995–8998, 1995. 86. K Murata, M Satake, H Naoki, HF Kaspar, T Yasumoto. Isolation and structure of a new brevetoxin analog, brevetoxin B2, from greenshell mussels from New Zealand. Tetrahedron 54:735–742, 1998. 87. T Seki, M Satake, L MacKenzie, HF Kaspar, T Yasumoto.

The type 1 congeners are the most abundant in nature, with PbTx-2 and PbTx3 being the most prevelant in G. breve. Although the ring systems in the middle of the molecules differ somewhat, type 1 and type 2 toxins share a lactone in the A ring (‘‘head’’) and a conserved structure on the ‘‘tail’’ ring, both of which are required for their toxicity (26). Type 2 congeners are more flexible (38 rotatable bonds) than those with the type 1 backbone (31 rotatable bonds), which may play a role in their generally greater potency (27).

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