Available online at www.jpsscientificpublications.

com

Life Science Archives (LSA)

ISSN: 2454-1354
Volume 1; Issue - 4; Year 2015; Page: 233 - 239

Research Article

NEUROMUSCULAR MODULATORY ACTIVITY OF LION FISH

Pterois russelii VENOM IN MICE
R. Saravanamurugan and A. Subramaniyan*
Department of Zoology, Annamalai University, Annamalai Nagar 608 002, Tamil Nadu, India.
Abstract
The present study was aimed to examine the impact of crude extract as well as partially purified
protein of lionfish venom on the neuronal system of mice. The treated mice were showed various behavioral
changes including miner shivering in fore limbs, loss of balance, opaque eyes, convulsions forming from
mouth and exophthalmia. It is possibly correlated with CNS and PNS dysfunction. The protein was found to
be modulate the functioning of the sodium pump (Na+, K+ and ATPase) at the presynaptic complex of neurotransmission, there by affecting ATP hydrolysis. They increase cholinesterase activity at the post synaptic
complex by modulating the activity of the enzyme Acetyl cholinesterase (AChE) and the modulation was
occurred in dose dependent manner. Histopathological observations revealed that the toxins were affected
the anatomy of the mice brain.
Key words: Lion fish, P. russelii, Proteins,
Article History
Received : 20.08.2015
Sodium pump, Acetylcholine, Neurotoxins and
Revised : 27.08.2015
Enzyme.
Accepted : 06.09.2015
1. Introduction

The activity of neuromuscular system is

vital for normal behavior and muscular function
and it represents a prime target system on which
some toxicants can produce a detrimental effect.
The excitability of sensory cells, neurons and
myocytes depends on ion channel and signal
transducers that provide a regulated path for the
movement of inorganic ions across the plasma
membrane in response to various stimuli. Ion
channels in plasma membrane are primary targets
of marine toxins. These channels are important
regulators of cell physiology and many of the
pathological effects of toxins result from the
modulation of ion channels.
* Corresponding author: A. Subramaniyan,
Department of Zoology, Annamalai University,
Annamalai Nagar.

Nerve cells are different from other cells

that they conduct bioelectrical signals for long
distance and possess intercellular connections with
neurons and other tissues. For proper functioning
of the neuron, it is essential that neurotransmission
should be maintained undisturbed. Drugs and
toxins that alter the normal processes of the
neurotransmission and are known to be
neuromodulators yielding beneficial or deleterious
effects on neuronal function. Therefore studies on
neuromodulatory effects of the venom are
worthful because of their profound usefulness in
pharmacological and neurophysiological studies.
ATPase activity is associated with the
active transport system, which is necessary for the
extrusion of Na+ from cells and the accumulation
of K+ within these cells. This enzyme is essential
for such function as the generator of cell volume
and electrolyte composition. Acetylcholine (ACh)

2015 Published by JPS Scientific Publications Ltd. All rights reserved

Subramaniyan / Life Science Archives (LSA), Volume 1, Issue 4, Page: 233 - 239, 2015
is a neurotransmitter that functions in conveying
nerve impulses across synaptic clefts within the
CNS (Tripathi and Sritvastava, 2008). Following
the transmission of an impulse across the synapse
by ACh, AChE is released into the synaptic cleft
(Horton et al., 2006). This enzyme hydrolyzes
ACh to choline and acetate and transmission of the
nerve impulse is terminated (Liesener et al.,
2007). Venoms and toxins represent useful tools to
investigate muscle degeneration and regeneration
since synchronic lesion can be induced by these
agents (Harris, 1992). The aim of the present study
is to know the modulation in ATP hydrolysis by
Na+, K+ and ATPase (sodium pump) and ACh
hydrolysis
by
acetylcholinesterase
in
neuromuscular junction and nerve ending by the
influence of toxins extracted from lionfish
P. russelii venom.
2. Materials and methods
Venom preparation
Live specimens of the venomous lionfish
P. russelii were collected from Mandapam coast
and brought to the laboratory. The fishes were
killed (by cooling) and the venomous spines were
removed and stored in 10% glycerol solution at 800C and the venom was extracted as described by
Church and Hodgson (2002). The venom protein
content was estimated by the method of Lowery et
al. (1951).
Behavioral study
Adult male Swiss albino mice (Mus
musculus) of 10 to 12 weeks old (22 2 g) were
obtained from the Central Animal House, Rajah
Muthiah Medical College, Annamalai University.
The animals were maintained under controlled
conditions of temperature (23 2 oC), humidity
(50 5%), and light (10 and 14 hrs of light and
dark cycles, respectively) and were fed with
commercial standard pellet and provided water ad
libitum. Animal handling and experimental
procedures were approved by the Institutional
Animal Ethics Committee, Annamalai University
(Registration Number: 953/2012/CPCSEA) and
the animals were cared in accordance with the
Guide for the care and use of laboratory animals

234

and Committee for the purpose of control and

supervision on experimental animals. The
lionfish venom at concentrations of 10 g/ml, 20
g/ml, 30 g/ml and 40 g/ml was administered
to experimental animals through single
intraperitoneal injection and control group was
maintained in each case by injecting an equal
volume of sterile saline. The time of injection and
death, in addition to behavioral changes before
death were recorded.
Neuromodulatory activity
In vitro studies
The effect of lionfish venom on mice brain Na+,
K+ and ATPase enzyme
Na+, K+ and ATPase were assayed in mice
brain by the method of Shalom and Katyare
(1985) and the inorganic phosphate released was
measured by the method of Fiske and Subbarow
(1925). The assay mixture consisting of 1ml
buffer, 0.2 ml magnesium sulphate, 0.2 ml
potassium chloride, 0.2 ml sodium chloride, 0.2
ml EDTA and 0.2 ml of tissue homogenate was
prepared. The reaction was started by the addition
of 0.2 ml ATP and was incubated. Then, the
contents were incubated at 37 C for 15 min. At
the end of 15 min, 1 ml of 10% TCA was added to
arrest the reaction. The enzyme activity was
expressed as moles phosphorous liberated / min/
mg/ protein / hour.
The effect of lionfish venom on mice brain
AChE (Acetylcholinesterase) enzyme
AChE activity was assayed in mice brain
using the method of Ellman et al. (1961). Brain
isolated from the albino mice was homogenized in
0.25 M ice cold sucrose and 2 % (W/V) tissue
homogenate was prepared in the same sucrose
solution and kept aside as enzyme source. Three
ml phosphate buffer (pH 8.0) was taken in each
test tube, to which 0.1 ml of 2 % homogenate was
added and stirred. A volume of 100 l of 0.01 M
DTNB was added and the initial color was
measured at 412 nm. The test solution, 20 l of
acetylthiocholineiodide (0.075 M) was allowed to
continue for 15 minutes at room temperature. The

2015 Published by JPS Scientific Publications Ltd. All rights reserved

Subramaniyan / Life Science Archives (LSA), Volume 1, Issue 4, Page: 233 - 239, 2015
color developed was measured at 412 nm in
spectrophotometer.


100
=
Absorbance of the standard
Amount of protein in the sample
incubation time in minutes

235

diarrhea, lethargy, dragging of hind limbs, rolling

of tail, foaming from mouth and exophthalmia.
Neuromodulatory activity
The effect of lionfish venom on mice brain Na+,
K+ and ATPase enzyme activity

The enzyme activity was expressed as moles

of AChE hydrolyzed per mg protein per hour.
Histopathological analyses
The histopathological changes were
observed in mice brain by the standard
histological methods of Luna, 1968. The brain was
removed carefully after the animals died and
immersed in 10% buffered formalin at room
temperature and then they were dehydrated in a
graded series of alcohol and xylene, embedded in
paraffin wax and then sectioned transversely into
3 4 m slices. Multiple slices were made and
stained by hematoxylin and eosin stains.
Histopathological changes were observed under a
light microscope.
Statistical Analysis
The experimental data were expressed as
means Standard Deviations. Differences in
means were estimated by using SPSS 16.0. Oneway analysis of variance (ANOVA) followed by
Duncans Multiple Range Test (DMRT) were
done. In all cases statistical significance is
indicated by P < 0.05.
3. Results
Behavioral changes in mice
After treating the mice with lionfish
venom, they showed the following behavioral
changes like lying on belly with forelimbs spread
wide, running around the cage in an exited
manner, escape reaction, prolonged palpitation,
closed eyes, grooming, shivering of forelimbs,
loss of balance, opaque eyes, squeaking, tonic
convulsions, gasping for breath, arching of body
backwards, paralysis, micturiction, flexing of
muscles, prodding (insensitive to stimuli),

The Table - 1 show the changes in the

activity of Na+, K+ and ATPase in mice brain. It
was revealed that with the increase in
concentration of P. russelii venom an increase in
Na+, K+and ATPase activity was observed. At 10
g/ml concentration of P. russelii venom, the
value was 12.46 0.37 moles /min/mg of
protein. The value increased to 12.86 0.46 at 20
g/ml concentration of P. russelii venom and
14.34 0.55 at 30 g/ml concentration of P.
russelii venom. At 40 g/ml concentration of P.
russelii venom the value was high 15.26 0.45
moles/min/mg protein.
Table 1: The effect of lionfish venom on mice brain
Na+, K+ and ATPase enzyme

Concentration
of venom
(g/ml)
Control
10
20
30
40

Na+, K+, ATPase activity

M Pi liberated min /mg
/protein
8.160.40
12.460.37*
12.860.46*
14.340.55*
15.260.45*

(Values are mean SD, n=6, * P < 0.05, control and venom
treated animal)

The effect of lionfish venom on mice brain

AChE (Acetylcholinesterase) enzyme activity
An elevated level of AChE was observed
in brain of mice treated with different doses of
crude P. russelii venom. The increase in activity
observed was dose dependent (Table 2).
The histopathological changes in the
venom treated mice revealed that the main organ
brain was affected by lionfish venom. The
histological section of the control mice brain
tissue showed a regular and compact configuration
with blood sinusoids. But, in the treated mice they
were highly congested with haemolyzed blood and
haemorrhage. Glial nodule formation was
observed in some areas of the cerebrum. The mild

2015 Published by JPS Scientific Publications Ltd. All rights reserved

Subramaniyan / Life Science Archives (LSA), Volume 1, Issue 4, Page: 233 - 239, 2015
congestion of capillaries and pycnotic nuclei, a
condition formed by the condensation of
chromatin in the nucleus of cell undergoing
necrosis were found in the cerebellum (Fig - 1).
Table 2: The effect of lionfish venom on mice brain
AChE (Acetylcholinesterase) enzyme

Concentration
of venom
(g/ml)
Control
10
20
30
40

AChE activity in Brain

M Ach hydrolyzed /mg
/protein/hour
0.280.02
0.310.03*
0.400.03*
0.630.01*
0.710.05*

(Values are mean SD, n=6, * P < 0.05, control and venom
treated animal)

Normal brain

Venom treated brain

A.Congested blood sinusoids,
B.Pycnotic nuclei,
C.Vacoulation,
D.Necrosis.
Fig- 1: Histopathological effects of P. russelii venom
on mice brain.

236

4. Discussion
The present study reveals that the toxin of
the lionfish altered the hydrolysis of ATP by Na+,
K+ and ATPase in the pre-synaptic region there by
possibly affecting signaling to intercellular
organelles. Our study is similarly with the study of
Xie and Askari (2002) and electrolyte movement
across epithelial cells (Ewart and Klip, 1995).
Some behavioral changes enlisted above such as
flexing of muscles, tonic convulsions, arching of
body backwards, paralysis might be due the
accumulation of AChE and total termination of
neuronal signaling (Zhang et al. ,2005) and also
increase in AChE was corroborated with
neuromuscular
paralysis
and
death
by
asphyxiation (Silman et al.,1988).
The membrane-bound enzyme ATPase
plays an important role in the maintenance of
membrane potentials and it has been estimated
that it accounts for upto 50 % of oxidative
metabolism in the brain and was deeply involved
in cellular function (Ratnakumari et al., 1995).
Membrane Na+, K+and ATPase plays an important
role in active transport of Na+ and K+ ions across
the plasma membrane. The enzyme was present in
high concentration in brain and muscle. Na+, K+
and ATPase is ubiquitous in nature in the
mammalian central nervous system and it was
found predominantly in glial and nerve terminals
(Chen et al., 2005). The sodium gradient is
important for the uptake of neurotransmitters into
nerve cells and glia, which suggests that the
changes in Na+, K+ and ATPase activity result in
the modulation of neurotransmission (Fighera et
al., 2006; Sivan, 2007). This enzyme activity has
been used as a potential indicator for membrane
toxicity (Engelke et al., 1992).
The observed increase in the activity of
+
Na , K+ and ATPase by P. russelii venom
suggests the presence of antinociceptive substance
in the venom. The increase in activity was dose
dependent. A similar increase in the enzyme
activity was observed by morphine and P.
valitance venom in the mouse brain (Masocha et
al., 2002; Balasubashini et al., 2006). Acetyl
cholinesterase (AChE) enzyme involved in the
hydrolysis of the neurotransmitter acetylcholine

2015 Published by JPS Scientific Publications Ltd. All rights reserved

Subramaniyan / Life Science Archives (LSA), Volume 1, Issue 4, Page: 233 - 239, 2015
and contributes to the integrity and permeability of
the synaptic membrane that occurs during
neurotransmission and conduction (Grafius et al.,
1971). This enzyme has been implicated in
cholinergic and non-cholinergic actions, which
may play a role in neurodegenerative diseases
(Cummings, 2000; Law et al., 2001; Habila et al.,
2012). Likewise, puffer fish Arothron hispidus
exhibited positive modulation in Na+, K+ and
ATPase, Mg++, ATPase and AChE enzyme
activity (Bragadeeswaran et al., 2010). The effect
of P. russelii venom on the AChE activity in mice
brain revealed that fish venom increases the
activity of enzyme in a dose dependent manner.
This may be either due to presence of
acetlycholine (Garnier et al., 1995) or by the
massive release of acetylcholine from the nerve
terminal that potentiates the activity of the enzyme
in mouse brain (Church and Hodgson, 2002).
Cohen and Olek (1989) have concluded
that the cellular action of toxin is by inducing
massive release and subsequent depletion of
acetylcholine
from
the
nerve
terminal.
Experiments with rat synaptosomes revealed that
stonefish venom affects neurotransmission and has
demonstrated the stimulation of release of the
neurotransmitter acetylcholine (Khoo et al., 1992).
The soldier fish G. marmoratus stimulate the
release of AChE to act at muscarinic receptors on
guinea - pig, gastrointestinal smooth muscle
(Hopkins et al., 1997). Trachynilysin (TLY)
isolated from Sirachynisvenom enhances the
release of acetylcholine from atrial cholinergic
nerve terminals (Colasante et al., 1996; Sauviat et
al., 2000; Ouanounou et al., 2000). The crude
venom exhibited neurostimulatory response on
mice brain AChE activity and the inhibitory effect
on AChE activity ranging between 23 % and 39 %
were caused by venom of C. lentiginosus (Pawan
Kumar et al., 2014).
Various lines of evidence strongly suggest
that the P. russelii venom was affected the
neuronal system functioning in mice. The brain of
mice that died upon the lionfish toxin
envenomation was due to the enlargement of
capillaries and glial nodules.
The foci of

237

microglia in degenerating neurons were found

particularly in the cerebrum. Mild congestion of
capillaries and pycnotic nuclei, a chromatin in the
nucleus of a cell undergoing necrosis were found
in the cerebellum. Similar observations were
reported by Ravindran et al. (2010) in the sea
anemone extracts administrated to mice.
The
histopathological
changes
in
P. russelii venom treated mice brain was the
vascular endothelium appeared to be injurious and
caused congestion of blood vessels and cloudy
swellings.
Brain tissue showed spongiosis
(oedema) throughout the parenchyma. Congested
blood vessels, spongiosis, pycnotic nuclei, glial
cell accumulation, focal area necrosis state was
due to the neurotoxicity of P. russelii venom. The
similar results were observed in Bungarus
caeruleus envenoming. Considering the site and
the mode of action of this poison on tissue level,
this findings may contribute for the discovery of
antivenom related valuable pharmaceutical
products (Al-Mamun et al., 2015).
5. Conclusion
The present study demonstrated that the
marine lionfish P. russelii venom protein have
potent pharmacological properties without any
series of toxic effects at low dosage level. Hence,
such protein could be used against cholinesterase
inhibitors and neuromodulatory drugs can be
developed from lionfish venom. These finding
strengthen the health care industry for the
development of indigenous medicine and it can be
used as remedies for analgesic and neurological
disorder.
Acknowledgement
The authors thankful the University Grand
commission, New Delhi (India) for financial
assistance.
6. References
1) Al-Mamun M. A., Rahman M. A., Hasan R.,
Rahmann Z., Haque K. M. F., (2015).
Histopathological alterations induced by
common krait Bungarus caeruleus venom on
hepatic, renal and cardiac tissues of albino

2015 Published by JPS Scientific Publications Ltd. All rights reserved

Subramaniyan / Life Science Archives (LSA), Volume 1, Issue 4, Page: 233 - 239, 2015

2)

3)

4)

5)

6)

7)

8)

9)

mice.Int. J. Pharm and Pharmaceutical

Sciences.Vol 7, Issue 1.
Balasubashini,
M.,
Karthigayan,
S.,
Somasundaram, S.T., Balasubramanian, T.,
Viswanathan, P. and Menon, V. P. (2006). In
vivo and in vitro characterization of the
biochemical and pathological changes induced
by lionfish Pterios volitans venom in mice.
Toxicology Mechanisms and Methods. 16: 525
- 531.
Bragadeeswaran, S, Therasa D, Prabhu K,
Kathiresan K., (2010). Biomedical and
pharmacological potential of tetrodotoxinproducing bacteria isolated from marine
pufferfish Arothron hispidus Muller, 1841. J.
Venom. Ani. Toxi. inclu. Tropi. Dis. 16:(3)
421-431.
Chen, P. W., Liu, S. H., Hsu, C. J. and LiuShiau, S. V. (2005). Correlation of increased
activities Na+, K+ ATPase and Ca+ ATPase
with the reversal of cisplatin ototoxicity
induced by D-methionine in guinea pig.
Hearing Res., 205: 102 - 109.
Church, J.E. and Hodgson, W.C. (2002). The
pharmacological activity of fish venoms.
Toxicon., 40:1083 -1093.
Cohen, A.S. and Olke, J. (1989). An extract of
lionfish (Pterois valitans) spine tissue contains
acetylcholine and a toxin that affects
neuromuscular transmission. Toxicon, 27 (12):
1367 1376.
Colasante, C. Meunier, F.A. Kreger, A.S. and
Molgo, J. (1996). Selective depletion of clear
synaptic vesicles and enhanced quantal
transmitter release at frog motor nerve endings
produced by trachynilysin, a protein toxin
isolated from stonefish (Synanceia trachynis)
venom. Eur. J. Neuroscrl, 8: 2149 - 2156.
Cummings, J. L. (2000). The role of
cholinergic agents in the management of
behavioral disturbances in AIzheimers
disease. Int. J. Neuropsycho pharmacol., 3:21
- 29.
Ellman, G.L., Coutney, K.D., Andres, V. and
Featherstone, R.M. (1961). A new and rapid
colorimetric determination of Acetylcholine
esterase activity. Biochem. Pharmacol,
7:
88 - 95.

238

10) Engelke, M., Diehl, H. and Tahti, H. (1992).

Effects of toluene and dn-hexane on rat
membrane fluidity and integral enzyme
activities. Pharmacol. Toxicol, 71: 343 347.
11) Ewart S.H. and Klip A, (1995). Hormonal
regulation of the Na+, K+ ATPase:
Mechanisms underlying rapid and sustained
changes in pump activity, Am J Physiol, 269C
295.
12) Fighera, M. R., Royes, L. F. F., Furian, A. F.,
Oliviera, M. S., Fiorenza, N. G., Filho, R. F.,
Petry, J. C., Coelho, R. C. and Carlo, F. M.
(2006). GM1 gangliosides prevent seizures,
Na+, K+ ATPase activity inhibition and
oxidative stress induced by glutaric acid and
pentylenetetrazole. Neurobioi. Dis.ln press.
13) Fiske, C.H. and Subbarow, Y. (1925). The
Colorimetric determination of phosphorus. J.
Biol. Chem, 66: 375 400.
14) Garnier, P., Goudey-Perriere, F., Breton, P.,
Dewulf, C., Petek, F. and Perriere, C. (1995).
Enzymatic properties of the stonefish [S.
verrucosa Bloch and Schneider, 1801] venom
and purification of a lethal, hypotensive and
cytolytic factor. Toxicon., 33: 143 - 155.
15) Grafius, M. A., Bond, H. E. and Millar, D. B.
(1971). Acetyl cholinesterase interaction with
a lipoprotein matrix. Eur. J. Biochem, 22: 382
- 390.
16) Habila N., Inuwa H.M., Aimola I.A., Lasisi
O.I., Muhammad A., Okafor A. I., Williams
I.S., (2012). Acetylcholinesterase activity in
the brain and blood of mice infected with Naja
nigricolis venom. Biological Segment: 3(1)
BS/1565.
17) Harris, J.B. (1992). Natural toxins in study of
degeneration and regeneration of skeletal
muscle. in: Methods in Neurosciences, Vol. 8,
Neurotoxins [Ed. P.M.Conn] San Diego.
Academic Press, pp.298 - 310.
18) Horton, H.T., Moran, L.A., Scrimgeour, K.G.,
Perry, M.D., Rawn, D.J., (2006). Principles of
Biochemistry 4th ed. Pearson Int. ed. pp 147.
19) Hopkins, B. J., Hodgson, W.C. and
Sutherland, S.K., (1997). An in vitro
pharmacological examination of venom from
the soldier fish Gymnapistes marmoratus.
Toxicon, 35: 1101 - 1111.

2015 Published by JPS Scientific Publications Ltd. All rights reserved

Subramaniyan / Life Science Archives (LSA), Volume 1, Issue 4, Page: 233 - 239, 2015
20) Khoo, H.E., Yuen, R., Poh, C.H. and Tan,
C.H. (1992). Biological activities of Synanceia
horrida [Stonefish] venom. Nat. Toxins., 1: 54
- 60.
21) Law, A., Gauthier, S. and Quirion, R. (2001).
Say NO Alzheimer's disease: the putative links
between nitric oxide and dementia of the
Alzheimers type. Brain Res. Rev.,
35:
73 - 96.
22) Liesener, A., Perclive, A., Schoni, R., Schebb,
N.H., Wilmer, M., Karst, U., (2007).
Screening of acetylcholinesterase inhabitors in
snake venom by electro spraying mass
spectrometry. Pure Appl. Chem. 79, 2339
2349.
23) Lowry, O.H., Rosebrough, N.J., Farr, A.L.,
Randal, R.J., (1951). Protein measurement
with Folin-phenol reagent. J. Biol. Chem.,
193:265 - 275.
24) Luna, L.G., 1968. Manu. Histol. Stain. Armed.
Forces. Inst. Pathol. McGraw- Hill Book
Company, New York, NY. p. 258.
25) Masocha, W., Gonzaliz, L. G., Baeyens, J. M.
and Agil, A. (2002). Mechanism involved in
morphine-induced activation of synaptosomal
Na+, K+ ATPase. Brain Res,
957: 311
- 319.
26) Ouanounou, G., Mattel, C., Meunier, F.A.,
Kreger, A.S. and Molgo, J. (2000).
Trachynilysin, a protein neurotoxin isolated
from stonefish Synanceia trachynis venom,
increases spontaneous quantal release from
Torpedo marmorata neuromuscular junction.
Cybium, 24: 149 -156.
27) Pawan Kumar, K. Venkateshvaran, P. P.
Srivastava, S. K. Nayak, S. M. Shivaprakash,
S. K. Chakraborty, (2014). Pharmacological
studies on the venom of the marine snail
Conus lentiginosus Reeve, 1844. International
Journal of Fisheries and Aquatic Studies.
1(3): 79-85.
28) Ratnakumari, L., Aude, R., Quershi, I. A. and
Butterworth, R. F. (1995). Na+, K+ ATPase
acitivies are increased in brain both in
congenital and acquired hyperammonemia
syndromes. Neurosci. Lett., 197: 89 - 92.
29) Ravindran, V.S, Kannan L & Venkateshvaran,
K, (2010). Biological activity of sea anemone

239

protein. I. Toxicology and Histopathology.

Indian J.Exp.Biol, 48: 1225.
30) Sauviat, M.P., Meunier, F.A., Kreger, A. and
Molgo, J. (2000). Effects of trachynilysin, a
protein isolated from stonefish [Synanceia
trachynis] venom on frog atrial heart muscle.
Toxicon., 38: 945 - 959.
31) Shallom, J.M. and S.S. Katyare, (1985).
Altered synaptosomal ATPase activity in rat
brain following prolonged in vivo treatment
nicotine. Biochem. Pharmacol, 34: 3445-3449.
32) Silman I. and Futerman A.H. (1988). Modes of
attachment of acetylcholinesterase to the
surface membrane, Eur. J. Biochem, 170: 11.
33) Sivan,
G.,
Venketesvaran,
K.
and
Radhakrishnan, C.K. (2007). Biological and
Biochemical properties of Scatophagus argus
venom, Toxicon., 50 : 563-571.
34) Tripathi, A., Srivastava, U.C., (2008).
Acetylcholineasterase: A versatile enzyme of
the nervous system. Annals of Neurosci. 15,
106 110.
35) Xie Z. and Askari A, (2002). Na+ K+ ATPase
as a signal transducter, Eur J. Biochem, 269:
2434.
36) Zhang D. and McCammon J.A, (2005). The
association of tetrameric Acetylcholinesterase
with Co1Q Tail: A Block Normal Mode
Analysis, Plos Comput Biol, 1: 6.

2015 Published by JPS Scientific Publications Ltd. All rights reserved