Handbook of Venoms and Toxins of Reptiles

Handbook of Venoms and Toxins of Reptiles

Language: English

Pages: 528

ISBN: 0849391652

Format: PDF / Kindle (mobi) / ePub


The Handbook of Venoms and Toxins of Reptiles offers "one-stop shopping" to all biologists, biochemists, toxicologists, physicians, clinicians, and epidemiologists, and informed laypersons interested in the biology of venomous reptiles, the biochemistry and molecular biology of venoms, and the effects and treatment of human envenomation. This book examines the topic generally, provides an overview of the current taxonomy of these reptiles, explains the similarities and differences in the venom delivery apparatus in different groups of reptiles, reviews state-of-the-art knowledge about specific venom components and their action, and summarizes effects of envenomation and treatment in humans on different continents.

Produced by leading toxinologists, biologists, biochemists, and physicians from 12 countries, the book provides a broad, international perspective that bridges divergent areas in modern biology. A synthesis of current knowledge about venoms and venomous reptiles, it contains a wealth of illustrations, including an 8-page color insert, that present a view of reptile toxinology from the whole animal to the glands producing venoms to the molecular models and the mechanisms of actions of the toxins themselves.

The book provides a context for understanding the range of activities present in venoms and supplies detailed information on many enzymes and toxins found in them, bringing into focus the worldwide extent of the occurrence and complexity of human envenomations by reptiles. It explores the unique and interesting results produced by collaborations between specialists from very different fields and how they can stimulate new and continued interest in research on venoms and the animals that produce them.

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cleaves both chains, most TL-SVSPs cleave either the α or β chain, releasing fibrinopeptide A (FPA) or fibrinopeptide B (FPB), respectively. Based on this activity, TL-SVSPs have been further classified into A, B, and AB classes (Pirkle, 1998). To date, most TL-SVSPs isolated are of the class A subtype. Examples of class AB TL-SVSPs include bilineobin isolated from Agkistrodon bilineatus and brevinase isolated from Agkistrodon blomhoffii brevicaudus (Komori et al., 1993; Lee et al., 1999). Fibrin

venom. Toxicon 23:255–69. Serrano, S. M. T., and R. C. Maroun. 2005. Snake venom serine proteinases: Sequence homology vs. substrate specificity, a paradox to be solved. Toxicon 45:1115–32. Serrano, S. M., J. D. Shannon, D. Wang, A. C. Camargo, and J. W. Fox. 2005. A multifaceted analysis of viperid snake venoms by two-dimensional gel electrophoresis: An approach to understanding venom proteomics. Proteomics 5:501–10. Siigur, J., U. Arumae, T. Neuman, E. Siigur, and M. Saarma. 1987. Monoclonal

and the interpretation of toxinological research data. In contrast, correct species-level taxonomy is of fundamental importance for the interpretation and replication of toxinological and medical research. Misidentified or unidentifiable venoms lead to wasted research effort (e.g., by researchers failing to find compounds of interest because they have been misled by sloppy taxonomy in another paper) and potentially to ineffective antivenoms and unnecessary snakebite fatalities (Warrell, 2008).

concluded that the similar species P. oligolepis and P. affinis are junior synonyms of P. laticeps. B. Superfamily Elapoidea 1. Lamprophiidae Atractaspis—Stiletto Snakes Members of the genus Atractaspis occur mostly in sub-Saharan Africa, with a limited distribution in Israel and the Arabian Peninsula. The taxonomy of the genus remains in a state of dis­ array due to the lack of comprehensive revisions and the paucity of material of most species. Trape 44 Handbook of Venoms and Toxins of

Pinto, A. F. M., L. Ma, B. Dragulev, J. A. Guimaraes, and J. W. Fox. 2007b. Use of SILAC for exploring sheddase and matrix degradation of fibroblasts in culture by the PIII SVMP atrolysin A: Identification of two novel substrates with functional relevance. Arch. Biochem. Biophys. 465:11–15. Reichl, A. P., S. M. T. Serrano, C. A. M. Sampaio, and F. R. Mandelbaum. 1993. Hydrolytic specificity of three basic proteinases isolated from the venom of Bothrops moojeni for the B-chain of oxidized insulin.

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