Metal and Nonprotein Constituents in Snake Venoms

Bieber, Allan L.

doi:10.1007/978-3-642-66913-2_9

Cited by 46 publications

(32 citation statements)

References 31 publications

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“…More than 26 enzymes have been found in snake venoms with proteolytic enzymes being the most common type [1,2]. The venom composition varies among individual of the same species due to many factors.…”

Section: Introductionmentioning

confidence: 99%

Proteomics of snake venoms from Elapidae and Viperidae families by multidimensional chromatographic methods

Nawarak

Sinchaikul

et al. 2003

Electrophoresis

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Snake venoms contain a large number of biologically active substances and the venom components are very useful for pharmaceutical applications. Our goal is to separate and identify components of snake venoms in ten snake species from the Elapidae and Viperidae families using multidimensional chromatographic methods. The multidimensional chromatographic methods include reversed-phase high-performance liquid chromatography (RP-HPLC), sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), lab-on-a-chip, two-dimensional electrophoresis (2-DE), and mass spectrometry. The venoms of eight snake species demonstrated major differences in hydrophobicity, molecular weight separations, and 2-DE protein distribution patterns. The 2-DE images showed major differences between families, within each family and even between the same species. Venoms of the Elapidae family showed many basic proteins with a wide range of molecular weights, while venoms of the Viperidae family showed wide ranges of pI and molecular weights, especially for Trimeresurus sp. The multidimensional chromatographic methods revealed specific differences in venom proteins intra-species as well as between species and families. We have isolated and identified proteins that may be unique for each species for further studies in the proteome of snake venoms and their potentially use in the pharmaceutical applications.

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Section: Introductionmentioning

confidence: 99%

Proteomics of snake venoms from Elapidae and Viperidae families by multidimensional chromatographic methods

Nawarak

Sinchaikul

et al. 2003

Electrophoresis

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“…[1][2][3] The venom components known to vary with geographic location, season, and age of the snake [4][5][6][7][8] is not primarily for self-defense, but has a more important role in prey immobilization and its subsequent digestion. 2,[9][10][11] Hence, several digestive enzymes in venoms, in addition to their hydrolytic activity have evolved to interfere in diverse physiological processes that help in the immobilization of prey/victim.…”

Section: Introductionmentioning

confidence: 99%

The pharmacological role of nucleotidases in snake venoms

Dhananjaya

D'Souza

2010

Cell Biochemistry & Function

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Several hydrolytic enzymes of snake venom have evolved to interfere in various physiological processes, which are well defined. However, hydrolytic enzymes such as nucleotidases (5'nucleotidase, ATPase, and ADPase) are less studied and their pharmacological role in venoms is not clearly defined. Very few studies have shown the pharmacological importance of these endogenous purine release related enzymes in venoms. The near-ubiquitous distribution of these enzymes in venoms, suggests a significant role for these enzymes in envenomation. It is suggested that their major function is in the generation of purines (mainly adenosine)-a multitoxin. Therefore, it appears that these enzymes play a central role in liberating adenosine and through the action of adenosine help in prey immobilization. However, apart from this, these enzymes could also possess other pharmacological activities. Further research is needed to biologically characterize these enzymes in snake venoms, such that their role in venom is clearly established.

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“…This fraction also contains ribo¯avin, nucleosides, peptides, lipids and carbohydrates. 7 Snake venom proteins are either enzymes, toxins or nerve growth factors. The most important enzymes of snake venoms are phospholipase A2, amino acid oxidase, phosphodiesterase, proteolytic enzymes and arginine ester hydrolase.…”

Section: Introductionmentioning

confidence: 99%

Separation and purification of Echis coloratus venom and some biological and biochemical effects of the proteins

Al-Saleh

Ghneim

Haddad

et al. 2002

Cell Biochemistry & Function

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Crude venom of Echis coloratus was separated into seven protein fractions using 7% preparative native polyacrylamide gel electrophoresis. The effect of crude venom and seven venom protein fractions (F1-F7) from Echis coloratus on key metabolic activities of fibroblast cultures was investigated. Confluent cultures were incubated with the venom proteins for 3 h at 37 degrees C. The specific activity of phosphofructokinase, was significantly lowered upon incubation with the crude venom and with fractions 2, 3, 4 and 6. Citrate synthase activity was significantly lowered by the crude venom and by fractions 2 and 3. Glycogen phosphorylase activity was significantly increased by the crude venom and by fractions 2, 3, 4 and 6 leading to a significant concurrent drop in glycogen content. Creatine kinase activity was significantly increased by the crude venom and by fractions 3, 4, 5 and 6. Cellular ATP levels rose significantly upon incubation with the crude venom and with fractions 3, 4, 5 and 6. Incubation of cell sonicates with all the venom proteins did not significantly alter the activity or content of any of the studied parameters.

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Metal and Nonprotein Constituents in Snake Venoms

Cited by 46 publications

References 31 publications

Proteomics of snake venoms from Elapidae and Viperidae families by multidimensional chromatographic methods

Proteomics of snake venoms from Elapidae and Viperidae families by multidimensional chromatographic methods

The pharmacological role of nucleotidases in snake venoms

Separation and purification of Echis coloratus venom and some biological and biochemical effects of the proteins

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