Pharmacognostic and Biochemical Properties of Certain Biomarkers in Snake Venom
S. Justin Raj,
Biby. T. Edwin
Snake venom is a special liquid which is produced by the poison gland of the poisonous snake. Snake venoms generally consist of a complex mixture of substances, each of which may exhibit one or more distinct toxic actions. Many of these proteins are harmless to humans but some are toxic. Snake venoms effects include, anti-blood coagulation, neurotoxicity, mycotoxicity, nephrotoxicity, cardiotoxicity and necrotoxicity. Snake venom is hemolytic and neuropathic-type venom. The hemolysis venom is more effective than the neuropathic-type venom and it will work almost immediately to the prey. According to traditional system of medicine, snake venom is widely used in various disorders in skin and blood. It performs good antitumor activity. This study reports on its traditional, chemical and pharmacological properties such as antioxidant, anticancer and analgesic activity.
October 02, 2010; Accepted: January 17, 2011;
Published: April 27, 2011
Snake venoms are generally produced by specialized glands which are related
to salivary glands and are toxic to the prey (Kochva, 1987).
Snake venoms contain a large number of biologically active proteins and peptides
that are usually similar in structure but not identical to that of prey physiological
systems. Snake venom is a mixture of different enzymes and having toxic and
non-toxic activities, including pharmacological properties. The mechanism of
toxin secretion is highly conserved and diversification of matured toxin sequences
shows existence of multiple protein isoforms in the venom to adapt within prey
environment (Fry, 2005). A duct to the fang base, where
it is transported into the victim either by a groove in the fang or through
a fang duct delivers the venom, once produced. The marine organisms (Cone snails)
deliver their complex venom through a specialized radular tooth that serves
as both a harpoon and disposable hypodermic needle (Joseph
et al., 2010a). Cone snails are large group of recently evolved,
widely distributed marine molluscs of the family Conidae. The evolution of conotoxin
in the venom of predator snails may be influenced by selective pressures imposed
by the nature of the prey, with peptides mixtures from piscivorous, molluscivorous
and vermivorous snails exhibiting differences (Olivera,
1997; Ramasamy et al., 2011). The action
of venom is the combined effect of all components present in the venom and the
snakes escape the effect of own toxins due to specific resistance mechanism
and modulation of acetylcholine receptors. Compounds accumulate in living things
any time they are taken up and stored faster than they are broken down (metabolized)
or excreted (Joseph et al., 2010b). Many of the
most potent snake toxins have evolved highly specific targets, such as the neuromuscular
junction or components of the haemostatic system. Phospholipase A2
or phosphatide acylhydrolase 2, is hemolytic and myolytic present in snake venom
which results in damage to cell membranes, endothelium, skeletal muscle, nerves
and erythrocytes. It is an enzyme that catalyzes the hydrolysis of the acyl
group attached to the 2-position of intracellular membrane phosphoglycerides
(Shah et al., 2011). Snake venoms are widely
used to develop anti-venom vaccines and medicine for rescuing snake venom poisoning
patients. Presence of antibacterial molecules in the snake venom that would
protect the snakes during feeding. Some of the first reports about antibacterial
activity of snake venom was in 1948 and in 1968, involving Elapidae and Viperidae
venoms (White, 2000; Glaser, 1948)
. Enzymes and proteins are also very important bioactives in snake venom. Apart
from enzymatic proteins, antimicrobial peptides have also been purified in recent
studies. Cathelicidins isolated from Bungarus fasciatus and Ophiophagus
hannah have reported potent antimicrobial activity against many strains
of Gram negative bacteria (Wang et al., 2008;
Chen et al., 2009; San et
al., 2010). Russel Viper Venom (RVV) X and V enzymes and ecarin from
Echis carinatus venom are proteins used for factors X and V and prothrombin
determination in blood (Magalhaes et al., 1981;
Rosing et al., 2001). Due to their characteristics,
RVV enzymes have been used for the improvement of the detection of von Willebrand
disease (Gold et al., 2002; Nahas
et al., 1979) Venom molecules are good examples, such as in homeostasis,
where they act as pro- and anticoagulant factors and also as inducers and inhibitors
of platelet aggregation(Gornitskaia et al., 2003;
Markland, 1997; Braud et al.,
2000). Snake venom has been reported to include antioxidant, antibacterial,
hypotensive, cancer suppressive, anticoagulant and analgesic activity. This
study was aimed to present an overview of traditional, chemical and pharmacological
investigations of bioactives present in snake venom.
COMPOSITION OF SNAKE VENOM
Fresh snake venom is a slightly fishy smell of the egg-like viscous liquid
which color is always yellow, green or even colorless. Fresh snake venom is
neutral or weak acid and it will become alkaline when it is placed for a long
time. Water content 50 to 75%. When exposed to air, fresh venom is easy to produce
foam. The composition of the venom is complex. It differs from species to species.
The main ingredient is the toxic protein. Almost all venoms are composed of
approximately 90% proteins. It contains more than 20 kinds of enzymes and toxins
and all sorts of smaller molecules. Some toxins have multiple effects . Snake
venoms also contain several peptides. They may vary from presenting neurotoxic
(Mion et al., 2002; Francischetti
et al., 1997; Harvey, 2001) cardiotoxic (Tsetlin
and Hucho, 2004; Satora et al., 2003) or
even an inhibitory platelet profile (Fry and Wuster, 2004;
Russell, 1980; Rucavado et al.,
1995; Ducancel, 2002; Morris
et al., 1995). In addition, it also contains a number of amino acids,
carbohydrates, lipids, nucleosides, biological amines and metal ions (Heise
et al., 1995; Russell, 1980). The most important
components are the substances with a cytotoxic effect, the neurotoxins and the
CLASSIFICATION OF SNAKE VENOM
Two general types of toxins are known, neurotoxins and hemotoxins. Neurotoxic
venom attacks the victim's central nervous system and usually result in heart
failure and breathing difficulties. Cobras, mambas, sea snakes, kraits and coral
snakes are examples of snakes that contain mainly neurotoxic venom. After the
bite, local symptoms were not obvious, less bleeding, swelling and slight fever.
However, within a few hours after injury, the rapid systemic symptoms, patients
with anxiety excitement, groaning with pain, difficulty swallowing, difficulty
breathing, convulsions, respiratory muscle paralysis and the death will appear.
In addition, some scientists are now studying this neurotoxin can be used to
treat virus such as the rabies virus. Hemotoxic venom attacks the circulatory
system and muscle tissue causing excessive scarring, gangrene, permanent disuse
of motor skills and sometimes leads to amputation of the affected area. It can
cause rapid swelling of the bite wound, bleeding and pain. The skin will become
purplish, black and necrotic. After 6-8 h, it could be spread to the head, neck,
limbs and lower back. If the bite wound has not treated effectively within 4
h at last death will occur due to heart failure or shock. The Viperidae family
such as rattlesnakes, copperheads and cottomouths are good examples of snakes
that employ mostly hemotoxic venom. Some snakes contain venom that contains
combinations of both neurotoxins and hemotoxins. Snake venom proteins and polypeptides
are classified into superfamilies of enzymes and non-enzymatic proteins. The
members of each superfamily show similarity in their primary, secondary and
tertiary structures. Among non-enzymatic proteins, superfamilies of three-finger
toxins, serine proteinase inhibitors, C-type lectin-related proteins, atrial
natriuretic peptides and nerve growth factors have already been well characterized
(Zhong et al., 2006; Li et
al., 2005; Ferreira et al., 1970). L-Amino
acid oxidase, phospholipase A2, metalloprotease and ribonuclease
A are some examples of superfamilies of enzymes in this family (Takasaki
et al., 1988; Gong et al., 1998; Wei
et al., 2006; Wang et al., 2004; Wu
et al., 2001). Based on the structure, activity and components, crude
venom are also classified into cardiotoxin, neurotoxin, cytotoxin and myotoxin
(Guinea et al., 1983; Barbosa
et al., 2005).
TRADITIONAL USES OF SNAKE AND SNAKE VENOM
Among the earliest recorded use of snakes in Chinese medicine was the application of sloughed snake skin, described in the Shen Nong Ben Cao Jing (ca. 100 A.D.) It was originally applied in the treatment of superficial diseases, including skin eruptions, eye infections or opacities, sore throat and hemorrhoids. The use of snake gallbladder is first recorded in Ming Yi Bie Lu (Transactions of Famous Physicians; compiled by Tao Hongjing and written around 520 A.D.) which was an update of the Shen Nong herbal with double the number of ingredients. In addition to the gallbladder, the skin (fanpi) and the meat of a pit viper (Agkistrodon halys; fanshe) were used to treat skin diseases, pain and intestinal hemorrhage. There are at least three features of snakes that capture the attention of traditional healers: they have an incredible flexibility and speed, they shed their skin and certain snakes are extremely poisonous when they bite. The flexibility of snakes has suggested that they might be helpful in the treatment of stiffness, for example, arthritis. Two types of snakes, agkistrodon and zaocys, are currently used in several traditional and patent prescriptions for arthritis and they are sometimes soaked in alcohol to make an extract for stiff joints. The speed with which some snakes move indicated to traditional observers that as medicines their substance can move quickly around the body. Snakes are said to treat wind syndromes which tend to move around quickly. However, people are also cautioned not to consume snake wine when exposed to potentially pathologic wind, as the rapid movement of the snake medicine may aid the initial penetration of wind. Snakes which shed their skin has suggested that they have a regenerative quality for treating chronic skin problems. As a result, snake skin and whole snake are used in the treatment of skin diseases. This application is similar to the use of sloughed cicada skin for treating skin ailments. Acne, carbuncles, itching skin and psoriasis are examples of conditions that may respond to snake skin. Snake skin is also considered useful in reducing clouding (nebula) of the cornea, the skin of the eyes. Poisonous animals often cause paralysis when they bite and this is due to the presence of neurotoxins. They are then used medically by oral administration (which greatly reduces the toxicity) for the treatment of convulsions (by inhibiting intense muscle contractions). Also, some forms of paralysis are tonic in nature, that is, due to overcontraction of muscles and in such cases the nerve toxins can overcome paralysis. Agkistrodon (but not zaocys) is a poisonous snake used for epilepsy and paralysis. Scorpions and millipedes (scolopendra) are used similarly. Anti-convulsive activity is also ascribed to snake skin and cicada skin. In the Ben Cao Gang Mu it was said that Agkistrodon penetrates the bone to expel the pathogenic wind and alleviate convulsion and is the essential material for wind arthralgia, convulsion, scabies and malignant scabies-because it travels everywhere, outward to the skin and inward to the viscera. It was noted in Illustrated Materia Medica that Agkistrodon has a quicker effect in treating wind syndrome than that of other snakes. Several records in Chinese medical books indicate that snake slough is useful for malignant sores, such as mammary abscess and tumor, boils, carbuncles and furuncles. The slough is usually roasted and then used both internally and topically. Snake bile has long been valued as a tonic, characterized as such by its sweet aftertaste. It is used to make a special health drink at snake restaurants (which are today still found in southern China, Hong Kong and Taiwan). The bile of a snake to be eaten is mixed with some rice wine and consumed before the meal as an invigorating beverage and appetite stimulant. In the treatment of diseases, snake bile is used for whooping cough, rheumatic pain, high fever, infantile convulsion, hemiplegia, hemorrhoids, gum bleeding and skin infections. The antitussive action of bile from Hydrophis cyanocinctus (a sea snake) is one-ninth that of codeine when assayed in mice (adult human codeine dosage for treating cough is 20-30 mg). Snake bile is collected in spring and summer when the content of solids is highest. Snake gallbladder is sometimes combined with pinellia or citrus to produce an antitussive and phlegm-resolving powder for treatment of acute bronchitis. Snakes are also used in the treatment of cancer. The small agkistrodon is a common ingredient in modern treatments, especially for leukemia. A combination of Agkistrodon halys and Natrix trigrina (water snake), in the form of powder (3-5 g per day), it is used as an adjunct to herbal decoctions and drug to treat hepatoma. Snake venom is also sometimes used as medicine; recent research has shown that snake venom may have value in treating cardiovascular diseases and blood pressure. Anticoagulant properties have been identified and are especially prevalent in the vipers.
Anticoagulant activity: The crude venom of Pseudechis australis
shows a dose-dependent anticoagulant action on human blood in vitro using
computerized thromboelastography. Clot progress parameters (K and α) were
affected at low dose levels and had no effect on onset of coagulation parameters
(SP, R). At high dose there was a total anticoagulant effect. These results
generally shows the anti coagulant effects of venom (Dambisya
et al., 1995).
Anti-invasive activity: The human glioblastoma cell line (T98G) was
treated with contortrostatin or Colloidal Gold-TNF-alpha (CG-TNF-alpha) alone
or in combination. Vitronectin and fibronectin-dependent adhesion of untreated
and treated glioma cells were studied. Contortrostatin significantly decreased
cell adhesion to vitronectin and fibronectin. Contortrostatin binds to T98G
integrins in an RGD-dependent manner, whereas protein kinase C (PKC) appears
to be involved in CG-TNF-alpha actions, leading to inhibition of cell invasion.
The efficiency of contortrostatin in inhibiting cell invasion was enhanced by
combination with CG-TNF-alpha. The combined use of contortrostatin and CG-TNF-alpha
may have potential for malignant glioma therapy by effectively inhibiting glioma
cell invasion (Schmitmeier et al., 2000).
Anti tumour activity: Cerastes Cerastes Venom (CCV) from the Egyptian
desert, at a concentration of 7μg mL-1 kills in vitro
a significant number of mammary tumor virus-induced cells (≈55%) from
mouse within a period of 48h. CCV (1μg/mouse), administered once per week
directly into growing tumors for a period of 4 weeks, was found to reduce tumor
load by 54% and as a consequence the CCV-treated mice lived for more than 35
days longer than untreated mice. Histological and ultrastructural examination
of the cells and tumors, conclude that necrosis is most likely the underlying
mechanism by which CCV inhibited the growth of tumor cells both in vitro
and in vivo (El-Refael and Sarkar, 2009). The
diluted snake venom (Hydrophis spiralis) exhibited a significant antitumor
activity against EAC (Ehrlich Ascites Carcinoma cells) and detrimental toxicity
on the liver of the treated animals (Karthikeyan et al.,
Antimicrobial activity: A panel of eight PLA2 myotoxins purified
from crotalid snake venoms, including both Lys 49 and Asp 49-type isoforms were
found to express bactericidal activity, indicating that this may be a common
action of the group IIA PLA2 protein family. A series of 10 synthetic
peptide variants, based on the original C-terminal sequence 115-129 of myotoxin
II and its triple Tyr→Trp substituted peptide p115-W3, were characterized.
In vitro assays for bactericidal, cytolytic and anti-endotoxic activities
of these peptides suggest a general correlation between the number of tryptophan
substitutions introduced and microbicidal potency, both against Gram-negative
(Salmonella typhimurium) and Gram-positive (Staphylococcus aureus)
bacteria (Santamaria et al., 2005). Crude venoms
from Viperidae species demonstrated significant inhibition zones between 6.6-12.5
mm. Calloselasma rhodostoma showed the largest inhibition zones between
of 10.2-12.5 mm (San et al., 2010).
Analgesic activity: Crotamine, a neurotoxic protein has been purified
from Crotalus durissus terrificus venom by gel filtration on Sephadex
G-75. When injected (i.p. or s.c.) in adult male Swiss mice (20-25 g), it induced
a time-dose dependent analgesic effect which was inhibited by naloxone, thus
suggesting an opioid action mechanism. Extremely low dose (133.4 μg kg-1,
i.p., about 0.4% of a LD50) is more potent ( 30-fold) than morphine
(w/w) as an analgesic (Mancin et al., 1998).
Hemostatic activity: Venom proteins of the Viperidae snake family exert
often with a narrow specificity, activating, inactivating or other converting
effects on different components of the hemostatic and fibrinolytic systems.
Purified snake venom proteins have become valuable tools in basic research and
in hemostaseology. Procoagulant as well as anticoagulant venom components
have been identified in invitro tests. Smaller doses of procoagulant venom components
applied to large organisms as in the case of snake-bite accidents in humans
may cause a consumption coagulopathy with localized or generalized bleeding.
Highly purified, specific fibrinogen coagulant venom proteinases are used in
human medicine to produce therapeutic defibrinogenation (Meier
and Stocker, 1991).
Hypotensive activity: Vascular endothelial growth factor (VEGF165) exhibits
multiple effects via the activation of two distinct endothelial receptor tyrosine
kinases: Flt-1 (fms-like tyrosine kinase-1) and KDR (kinase insert domain-containing
receptor). KDR shows strong ligand-dependent tyrosine phosphorylation in comparison
with Flt-1 and mainly mediates the mitogenic, angiogenic and permeability-enhancing
effects of VEGF165. They also induced strong hypotension on rat arterial blood
pressure compared with VEGF165 in vivo (Yamazaki
et al., 2003).
Anti-Thrombotic activity: Snake venom act selectively on different blood
coagulation factors, blood cells or tissues. Venom proteins affect platelet
function in particular by binding and blocking or clustering and activating
receptors or by cleaving receptors. They may also activate protease-activated
receptors or modulate ADP release or thromboxane A2 formation. L-amino
acid oxidases activate platelets by producing H2O2. Many
of these purified components are valuable tools in providing new information
about receptor function and signaling (Clemetson et al.,
The present study shows the pharmacological and traditional properties of various bioactive compounds present in the venom. Snake venom is a good antibiotic. It is also a good medicine in traditional system, recent research has shown that snake venom may have value in treating cardiovascular diseases, reducing blood pressure and also have anticoagulant properties. Snake venoms also contain several peptides. snake venom peptides have the potential for practical and therapeutic use. However, enzymes and proteins are also very important as some of them are described as laboratory diagnosis reagents. However, more Clinical and Pathological studies should be conducted to investigate the active principles present in snake venom.
Barbosa, P.S., A.M. Martins, A. Havt, D.O. Toyama and J.S. Evangelista et al., 2005. Renal and antibacterial effects induced by myotoxin I and II isolated from Bothrops jararacussu venom. Toxicon, 46: 376-386.
Braud, S., C. Bon and A. Wisner, 2000. Snake venom proteins acting on haemostasis. Biochimie, 82: 851-859.
Chen, X.X., G.Y. Yu, Y. Zhan, Y. Zhang, J.H. Shen and W.H. Lee, 2009. Effects of the antimicrobial peptide OH-CATH on Escherichia coli. Zool. Res., 30: 171-177.
Clemetson, K.J., Q. Lu and J.M. Clemetson, 2007. Snake venom proteins affecting platelets and their applications to anti-thrombotic research. Curr. Pharm. Des., 13: 2887-2892.
Dambisya, Y.M., T.L. Lee and P. Gopalakrishnakone, 1995. Anticoagulant effects of Pseudechis australis (Australian king brown snake) venom on human blood: A computerized thromboelastography study. Toxicon, 33: 1378-1382.
Ducancel, F., 2002. The sarafotoxins. Toxicon, 40: 1541-1545.
Direct Link |
El-Refael, M.F. and N.H. Sarkar, 2009. Snake venom inhibits the growth of mouse mammary tumor cells in vitro and in vivo. Toxicon, 54: 33-41.
Ferreira, S.H., D.C. Bartelt and L.J. Greene, 1970. Isolation of bradykinin-potentiating peptides from Bothrops jararaca venom. Biochemistry, 9: 2583-2593.
Francischetti, I.M., B. Saliou, M. Leduc, C.R. Carlini and M. Hatmi et al., 1997. Convulxin, a potent platelet-aggregating protein from Crotalus durissus terrificus venom, specifically binds to platelets. Toxicon, 35: 1217-1228.
CrossRef | PubMed |
Fry, B.G. and W. Wuster, 2004. Assembling an arsenal: Origin and evolution of the snake venom proteome inferred from phylogenetic analysis of toxin sequences. Mol. Biol. Evol., 21: 870-883.
Fry, B.G., 2005. From genome to venome: Molecular origin and evolution of the snake venom proteome inferred from phylogenetic analysis of toxin sequences and related body proteins. Genome Res., 15: 403-420.
Glaser, H.R.S., 1948. Bactericidal activity of Crotalus venom in vitro. Copeia, 1948: 245-247.
Direct Link |
Gold, B.S., R.C. Dart and R.A. Barish, 2002. Bites of venomous snakes. N. Engl. J. Med., 347: 347-356.
Direct Link |
Gong, W., X. Zhu, S. Liu, M. Teng and L. Niu, 1998. Crystal structures of acutolysin A, a three-disulfide hemorrhagic zinc metalloproteinase from the snake venom of Agkistrodon acutus. J. Mol. Biol., 283: 657-668.
Gornitskaia, O.V., T.N. Platonova and G.L. Volkov, 2003. Enzymes of snake venoms. Ukr. Biokhim. Zh., 75: 22-32.
Guinea, M.L., N. Tamiya and H.G. Cogger, 1983. The neurotoxins of the sea snake Laticauda schistorhynchus. Biochem. J., 213: 39-41.
Harvey, A.L., 2001. Twenty years of dendrotoxins. Toxicon, 39: 15-26.
Heise, P.J., L.R. Maxson, H.G. Dowling and S.B. Hedges, 1995. Higher-level snake phylogeny inferred from mitochondrial DNA sequences of 12S rRNA genes. Mol. Biol. Evol., 12: 259-265.
Direct Link |
Joseph, B., M.V. Jeevitha, S.U. Ajisha and S.S. Rajan, 2010. Conotoxins: A potential natural therapeutic for pain relief. Int. J. Phar. Biol. Res.,
Joseph, B., S.J. Raj, B.T. Edwin, P. Sankarganesh, M.V. Jeevitha, S.U. Ajisha and S.R. Sheeja, 2010. Toxic effect of heavy metals on aquatic environment. Int. J. Biol. Chem. Sci., 4: 939-952.
CrossRef | Direct Link |
Karthikeyan, R., S. Karthigayan, M. Sri Balasubashi, S. Vijayalakshni and T. Balasubramanian, 2007. Antitumor effect of snake venom (Hydrophis spiralis) on ehrlich ascites carcinoma bearing mice. Int. J. Cancer Res., 3: 167-173.
CrossRef | Direct Link |
Kochva, E., 1987. The origin of snakes and evolution of the venom apparatus. Toxicon, 25: 65-106.
Li, W.F., L. Chen, X.M. Li and J. Liu, 2005. A C-type lectin-like protein from Agkistrodon acutus venom binds to both platelet glycoprotein Ib and coagulation factor IX/factor X. Biochem. Biophys. Res. Commun., 332: 904-912.
Magalhaes, A., G.J. de Oliveira and C.R. Diniz, 1981. Purification and partial characterization of a thrombin-like enzyme from the venom of the bushmaster snake, Lachesis muta noctivaga. Toxicon, 19: 279-294.
Mancin, A.C., A.M. Soares, S.H. Andriao-Escarso, V.M. Faca and L.J. Greene et al., 1998. The analgesic activity of crotamine, a neurotoxin from Crotalus durissus terrificus (South American rattlesnake) venom: A biochemical and pharmacological study. Toxicon., 36: 1927-1937.
PubMed | Direct Link |
Markland, Jr. F.S., 1997. Snake venoms. Drugs, 54: 1-10.
Meier, J. and K. Stocker, 1991. Effects of snake venoms on hemostasis. Crit. Rev. Toxicol., 21: 171-182.
Mion, G., F. Olive, E. Hernandez, Y.N. Martin, A.S. Vieillefosse and M. Goyffon, 2002. Action of venoms on blood coagulation: Diagnosis of hemorrhagic syndromes. Bull. Soc. Pathol. Exot., 95: 132-138.
Morris, V.L., E.E. Schmidt, S. Koop, I.C. MacDonald and M. Grattan et al., 1995. Effects of the disintegrin eristostatin on individual steps of hematogenous metastasis. Exp. Cell Res., 219: 571-578.
Nahas, L., A.S. Kamiguti and M.A. Barros, 1979. Thrombin-like and factor X-activator components of Bothrops snake venoms. Thromb. Haemost., 41: 314-328.
Olivera, B.M., 1997. Conus venom peptides, receptor and ion channel targets, and drug design: 50 million years of neuropharmacology. Mol. Biol. Cell, 8: 2101-2109.
Direct Link |
Ramasamy, M.S., P. Arumugam, S. Manikandan and A. Murugan, 2011. Molecular and combinatorial array of therapeutic targets from conotoxins. Am. J. Drug Discovery Dev., 1: 49-57.
CrossRef | Direct Link |
Rosing, J., J.W. Govers-Riemslag, L. Yukelson and G. Tans, 2001. Factor V activation and inactivation by venom proteases. Haemostasis, 31: 241-246.
Rucavado, A., G. Borkow, M. Ovadia and J.M. Gutierrez, 1995. Immunological studies on BaH1 and BaP1, two hemorrhagic metalloproteinases from the venom of the snake Bothrops asper. Toxicon, 33: 1103-1106.
Russell, F.E., 1980. Venoms. In: Snake Venom Poisoning, Lippincott, J.B. and G.M. Persol (Eds.). Lippincott, Philadelphia, pp: 139-234.
San, T.M., J. Vejayan, K. Shanmugan and H. Ibrahim, 2010. Screening antimicrobial activity of venoms from snakes commonly found in Malaysia. J. Applied Sci., 10: 2328-2332.
CrossRef | Direct Link |
Santamaria, C., S. Larios, Y. Angulo, J. Pizarro-Cerda, J.P. Gorvel, E. Moreno and B. Lomonte, 2005. Antimicrobial activity of myotoxic phospholipases A2 from crotalid snake venoms and synthetic peptide variants derived from their C-terminal region. Toxicon, 45: 807-815.
Satora, L., J. Morawska and D. Targosz, 2003. Cardiotoxicity of vertebrates venoms. Przegl. Lek., 60: 199-201.
Schmitmeier, S., F.S. Markland and T.C. Chen, 2000. Anti-invasive effect of contortrostatin, a snake venom disintegrin and TNF-α on malignant glioma cells. Anticancer Res., 20: 4227-4233.
Shah, B.N., A.K. Seth and K.M. Maheshwari, 2011. A review on medicinal plants as a source of anti-inflammatory agents. Res. J. Med. Plant, 5: 101-115.
CrossRef | Direct Link |
Takasaki, C., S. Kimura, Y. Kokubun and N. Tamiya, 1988. Isolation, properties and amino acid sequences of a phospholipase A2 and its homologue without activity from the venom of a sea snake, Laticauda colubrine, from the Solomon Islands. Biochem. J., 253: 869-875.
Tsetlin, V.I. and F. Hucho, 2004. Snake and snail toxins acting on nicotinic acetylcholine receptors: Fundamental aspects and medical applications. FEBS Lett., 557: 9-13.
Wang, W.J., C.H. Shih and T.F. Huang, 2004. A novel P-I class metalloproteinase with broad substrate-cleaving activity, agkislysin, from Agkistrodon acutus venom. Biochem. Biophys. Res. Commun., 324: 224-230.
Wang, Y., J. Hing, X. Lai, H. Yang and R. Liu et al., 2008. Snake cathelicidin from Bungarus fasciatus is a potent peptide antibiotics. PLoS ONE, 3: e3217-e3217.
CrossRef | Direct Link |
Wei, J.F., X.L. Wei, Q.Y. Chen, T. Huang and L.Y. Qiao et al., 2006. N49 phospholipase A2, a unique subgroup of snake venom group II phospholipase A2. Biochim. Biophys. Acta, 1760: 462-471.
White, J., 2000. Bites and stings from venomous animals: A global overview. Ther. Drug Monit., 22: 65-68.
Direct Link |
Wu, W.B., H.C. Peng and T.F. Huang, 2001. Crotalin, a vWF and GP Ib cleaving metalloproteinase from venom of Crotalus atrox. Thromb. Haemost., 86: 1501-1511.
Yamazaki, Y., K. Takani, H. Atoda and T. Morita, 2003. Snake venom Vascular Endothelial Growth Factors (VEGFs) exhibit potent activity through their specific recognition of KDR (VEGF receptor 2). J. Biol. Chem., 278: 51985-51988.
Zhong, S.R., Y. Jin, J.B. Wu, R.Q. Chen and Y.H. Jia et al., 2006. Characterization and molecular cloning of dabocetin, a potent antiplatelet C-type lectin-like protein from Daboia russellii siamensis venom. Toxicon, 47: 104-112.