Wasp Venom (<i>Polistes flavus</i>) Induced Bio-molecular and Enzymatic Alterations in Albino Mice and Its Reversal After Using Anti-venom

Krishna Kumar Prajapati; Ravi Kant Upadhyay

doi:doi:10.11648/j.ajbio.20221006.15

| Peer-Reviewed

Wasp Venom (Polistes flavus) Induced Bio-molecular and Enzymatic Alterations in Albino Mice and Its Reversal After Using Anti-venom

Krishna Kumar Prajapati, Ravi Kant Upadhyay

Published in American Journal of BioScience (Volume 10, Issue 6)

Received: 4 November 2022 Accepted: 25 November 2022 Published: 23 December 2022

Views: Downloads:

Download PDF

Share This Article

Twitter
Linked In
Facebook

Abstract

In the present investigation, in vivo effects of wasp toxin were evaluated on reversal of metabolic enzymes after providing purified anti-venom antibodies (anti-toxins) at 4 hour of treatment with 40% 24-h LD₅₀. Venom glands of yellow wasp Polistes flavus were homogenized and loaded on gel filtration column for purification and isolation of venom toxins/proteins from wasp Polistes flavus. These proteins were venom proteins ranging from 14.3-63 kDa. The yellow wasp venom proteins obtained from the lyophilization of the two peaks caused toxicity in the albino mice. The LD₅₀of the yellow wasp Polistes flavus venom protein was found 36.11 mg/kilogram body weight i.e., 0.03611 mg/gram body weight of albino mice. Presence of antibodies in antiserum was tested by using the immune-double diffusion method of Ouchterlony (1962). A precipitin ring was obtained by filling purified antigen and antibody interaction after 24 hrs. Albino mice were treated with 40% of 24-h LD₅₀ of purified wasp venom pre-incubated with different doses of purified wasp anti-venom and the neutralizing effects of anti-venom was measured in terms of reversal of metabolic alterations caused by wasp venom, after 4 hours of the treatment. The purified wasp anti-venom significantly (p<0.05) reversed the metabolic alterations caused by the wasp venom. The reversal of venom induced metabolic alteration in alkaline phosphatase, acid phosphatase, glutamate pyruvate transaminase, glutamate oxaloacetate transaminase, lactic dehydrogenase and acetylcholinesterase activity in the serum of albino mice was dose dependent (p<0.05, student t-test). This restoration of enzyme levels in blood serum, liver and gastrocnemius muscles of albino mice also display healing of liver damage, and necrosis in hepatic cells.

Published in	American Journal of BioScience (Volume 10, Issue 6)
DOI	10.11648/j.ajbio.20221006.15
Page(s)	206-219
Creative Commons	This is an Open Access article, distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution and reproduction in any medium or format, provided the original work is properly cited.
Copyright	Copyright © The Author(s), 2022. Published by Science Publishing Group

Keywords

Polistes flavus, Envenomation, Venom Toxins, Metabolic Alterations in Biomolecules, Enzymes, Restoration and Reversal of Toxicity, Immunotherapy

References

[1]	Jesmin, T., Muinuddin, G., Hossain, M. M., Rahman, M. H. and Mamun, A. A. (2013). Acute renal failure following wasp sting, Mymensingh Med J, 22 (3): 609-12.
[2]	Papini, R. A. (2014). A case of stings in humans caused by Sclerodermus sp. in Italy. J Venom. Anim. Toxins. Incl. Trop. Dis. 20 (1): 11.
[3]	Sturm, G. J., Kranzelbinder, B., Schuster, C., Sturm, E. M., Bokanovic, D., Vollmann, J., Crailsheim, K., Hemmer, W. and Aberer, W. (2014). Sensitization to Hymenoptera venoms is common, but systemic sting reactions are rare. J. Allergy. Clin. Immunol. 133 (6): 1635-43.
[4]	Krishna, K. P., Ravi K. U. (2019). In vivo effects of the purified venom of Polistes flavus on blood Biomolecules in albino mice. Internal Journal of Research and Analytical rewiev. June 2019 volume 6, Issue 2. E-ISSN 2348-1269, P-ISSN 2349-5138, pp 132-147.
[5]	Xie, C., Xu, S., Ding, F., Xie, M., Lv, J. and Yao, J. (2013). Clinical features of severe wasp sting patients with dominantly toxic reaction: analysis of 1091 cases, 8 (12): e83164.
[6]	Moreau, S. J. M. (2013). It stings a bit but it cleans well. Venoms of Hymenoptera and their antimicrobial potential. J. Insect Physiol; 59: 186–204.
[7]	Yavuz, S. T., Sahiner, U. M., Buyuktiryaki, B., Soyer, O. U., Sackesen, C., Sekerel, B. E. and Tuncer, A. (2013). Clinical features of children with venom allergy and risk factors for severe systemic reactions, Int. Arch. Allergy. Immunol. 160 (3): 313-21.
[8]	Fenney, D. J. (1971). Probit analysis, 3rd ed. Cambridge University, London, U. K., pp. 333.
[9]	Lowry, O. H., Rosenbrough, N. J., Farr, A. L. and Randall, R. J. (1951). Protein measurement with phenol reagent. J. Biol. Chem., 193: 265- 275.
[10]	Spies, J. R. (1957). Colorimetric procedure for amino acids. In: Colowich SP, Kalpan NO eds. Methods in Enzymology. Academic Press.
[11]	Mendel, B., Kemp, A. and Mayers, D. K. (1954). A colorimetric micro-method for the determination of glucose. Biochem. J. 56: 639-645.
[12]	Friedman, T. E. and Haugen, G. E. (1943). Pyruvic acid II. The determination of keto acids in blood and urine. J. Biol. Chem., 147: 415-442.
[13]	Folin, O. (1933). Standard method for the determination of uric acid in blood and in urine. J. Biol. Chem., 101: 111-125.
[14]	Abell, L. L., Levy, B., Brodie, B. B. and Kendall, F. E. (1952). A simple method for the estimation of total cholesterol in serum and demonstration of its specificity. J. Biol. Chem., 195: 357.
[15]	Bergmeyer, U. H. (1967). Determination of alkaline phosphatase and acid phosphatase by using p-nitrophenyl phosphate. In: Method of enzymatic analysis, New York Academic Press, New York, 1129.
[16]	Reitman, A. and Frankel, S. (1957). A colorimetric method for the determination of glutamate oxaloacetate and serum glutamate pyruvate transaminase. Am. J. Clin. Pathol. 28: 56-63.
[17]	Annon, T. M. (1984). Sigma diagnostic: Lactate dehydrogenase (Quantitative, Colorimetric determination in serum, urine and cerebrospinal fluid) at 400-500 nm. Procedure No. 500.
[18]	Ellman, G. L., Courtney, K. D., Andres, V. and Featherstone, R. M. (1961). A new and rapid colorimetric determination of acetylcholinesterase activity. Biochem. Pharmacol. 7: 88-95.
[19]	Ouchterlony, O. (1962). Diffusion in gel methods for immunological analysis II. In: progress in allergy. (Kallos, P. and Waksman B. H. eds), Vol 6, Basal. Karger., pp. 30-154.
[20]	Jones, R. G., Corteling, R. L., Bhogal, G. and London, J. (1999). A novel Fab-based antivenom for the treatment of mass bee attacks. Am. J. Trop. Med. Hyg., 61, 361-366.
[21]	Natu, V. S., Radha Krishna Murthy, K. and Deodhar, K. P. (2006). Efficacy of species-specific anti-scorpion venom serum (AScVS) against severe, serious scorpion stings (Mesobuthus tamulus concannesis Pocock)- An experiences from rural hospital in Western Maharastra. J. A. P. I. 54, 283-287.
[22]	Vetter, R. S., Visscher, P. K. and Camazine, S. (1999). Mass Envenomation by honeybees and wasps. West. J. Med., 170 (4), 223-227.
[23]	Lima, P. R. M., Brochetto-Braga, M R. and Chaud,-Neto, J. (2000). Protiolytic activity of Africanized honeybee (Apis mellifera: hymenoptera, Apidae) venom. J. Venom. Anim. Toxins. 6, 64-76.
[24]	Sousa, J. R. F., Monterio, R. Q., Castro, H. C. and Zingali, R. B. (2001). Proteolytic action of Bothrops jararaca venom upon its own constituents. Toxicon., 39, 787-792.
[25]	Schmidt, J. O. (1986). Chemistry, pharmacological and chemical ecology of venoms. In: venoms of the hymenoptera (Piek, T. ed). Acadmic Press, London., pp. 425-508.
[26]	Krauze, M., Truchlinski, J. and Cendrowaka-Pinkosz, M. (2007). Some biochemical parameters of plasma of turkey-hens following administration of 1,2,4-triasole derivative. Pol. J. Vet. Sci., 10 (2), 109-112.
[27]	Zeba and Khan, M. A. (1995). Effects of fenvalerate on protein and amino acid contents and enzyme activity in the Ostracod. Chrissicahalyi. Pectic. Sci., 45: 279-282.
[28]	Meneshian, A. and Bulkely, G. B. (2002). The physiology of endothelial xanthine oxidase: from urate catabolism to reperfusion injury to inflammatory signal transduction. Micro circulation., 9, 161-175.
[29]	Leyva, F., Wingrove, C. S., Godsland, I. F. and Stevenson, J. C. (1998). The glycolytic pathway to coronary heart disease: a hypothesis. Metabolism., 47, 657-662.
[30]	Quinines, G. A., Natali, A. and Baldi, S. (1995). Effects of insulin on uric acid excretion in humans. Am. J. Physiol., 268, 1-5.
[31]	Daisley, H. (1988). Acute haemorrhargic pancreatitis following multiple stings by Africanized bees in Trinidad. Trans. R. Soc. Trop. Med. Hyg., 9, 71-72.
[32]	Buchler, M., Malfertheiner, P., Schadlich, H., Nevalainen, T. J., Friess, H. and Beger, H. G. (1989). Role of phospholipase A2 in human acute pancreatitis. Gastroenterology., 97, 1521-1526.
[33]	Scheuer, J. and Stejoskins, W. A. (1969). A protective effects of increased glycogen stores in cardiac anoxia. J. Lab. Clin. Med., 74, 1007-1013.
[34]	Murthy, R. K. and Haghanazari, L. (1999). The blood level of glucagons, cartisol and insulin following the injection of venom by the scorpion (Mesobuthus tumulus concanesis) in dogs. J. venom. Anim. Toxins., 5, 48-53.
[35]	Bouck, G. R. (1966). Changes in blood and muscles composition of rock bass (Ambloplites rupestris) as physiological criteria of stressful conditions. Ph. D. dissertation, Michigan State University, East Landing, Michigan, USA.
[36]	Srinivasan, K. N., Gopala krishnakone, P., Tan, P. T., Chew, K. C., Cheng, B. and Kini, R. M. (2002). Scorpion, a molecular database of scorpion toxins, Toxicon. 40 (1): 23-31.
[37]	Arkhypova, V. N., Dzyadevych, S. V., Soldatkin, A. P., El'skaya, A. V., Jaffrezic-Renault, N., Jaffrezic, H. and Martelet, C. (2001). Multibiosensor based on enzyme inhibition analysis for determination of different toxic substances. Talanta, 55 (5): 919-27.
[38]	Luskova, V., Svoboda, M. and Kolarova, J. (2002). The effect of diazinon on blood plasma biochemistry in crab (Cyprinus carpiol). Acta. Vet. Brono. 71: 117-123.
[39]	Abou-Donia, M. B. (1978). Increased acid phosphatase activity in hens following an oral dose of leptophos. Toxicol. Let., 2, 199-203.
[40]	Abraham, R., Goldberg, L. and Grasso, P. (1967). Hepatic response to lysomal effects of hypoxia, neutral red and chloroquine. Nature, 215: 194-196.
[41]	Pilo, B., Asnani, M. V. and Shah, R. V. (1972). Studies on wound healing and repair in pigeon liver II; Histochemical studies on acid and alkaline phosphatase during the process. J. Anim. Morphol. Physiol. 19, 205-212.
[42]	Hopkins, B. J. and Hodgson, W. C. (1998). Cardiovascular studies on venom from the soldierfish (Gymnapistes marmoratus). Toxicon. 36 (7): 973-83.
[43]	Lehninger, A. L., Cox, M. M. and Nelson, D. L. (2000). Principal of biochemistry. 2nd ed. Worth, Publishers, New York, N. K. pp. 633.
[44]	Schmidt, E. and Schmidt, F. W. (1974). The importance of enzymatic analysis in medicine. In: methods of enzymatic analysis, Vol. I (Bergmeyer, H. U. ed). Acadmic Press, New York., pp. 6-14.
[45]	Krajnovic-Ozretic, M. and Ozretic, B. (1987). Estimation of the enzymes LDH, GOT, and GPT in plasma of grey mullet, Mugil auratus and their significance in liver intoxication, Disease of Aquatic Organisms, 3, 187-193.
[46]	Omran, M. A. A. and Abel-Rahman, M. S. (1992). Effects of the scorpion Leiurus quinquestriatus (H&E) venom on the clinical chemistry parameters of the rat. Toxicol. Lett., 61. 99-101.
[47]	Fischer, E. H., Heilmeyer, L. M. G. and Hashcke, R. H. (1971). Phosphorylase and the control of glycogen degradation. Curr. Trop. Cell. Regul., 4, 211, 707-710.

Cite This Article

Plain Text BibTeX RIS

APA Style

Krishna Kumar Prajapati, Ravi Kant Upadhyay. (2022). Wasp Venom (Polistes flavus) Induced Bio-molecular and Enzymatic Alterations in Albino Mice and Its Reversal After Using Anti-venom. American Journal of BioScience, 10(6), 206-219. https://doi.org/10.11648/j.ajbio.20221006.15

Copy | Download

ACS Style

Krishna Kumar Prajapati; Ravi Kant Upadhyay. Wasp Venom (Polistes flavus) Induced Bio-molecular and Enzymatic Alterations in Albino Mice and Its Reversal After Using Anti-venom. Am. J. BioScience 2022, 10(6), 206-219. doi: 10.11648/j.ajbio.20221006.15

Copy | Download

AMA Style

Krishna Kumar Prajapati, Ravi Kant Upadhyay. Wasp Venom (Polistes flavus) Induced Bio-molecular and Enzymatic Alterations in Albino Mice and Its Reversal After Using Anti-venom. Am J BioScience. 2022;10(6):206-219. doi: 10.11648/j.ajbio.20221006.15

Copy | Download

@article{10.11648/j.ajbio.20221006.15,
  author = {Krishna Kumar Prajapati and Ravi Kant Upadhyay},
  title = {Wasp Venom (Polistes flavus) Induced Bio-molecular and Enzymatic Alterations in Albino Mice and Its Reversal After Using Anti-venom},
  journal = {American Journal of BioScience},
  volume = {10},
  number = {6},
  pages = {206-219},
  doi = {10.11648/j.ajbio.20221006.15},
  url = {https://doi.org/10.11648/j.ajbio.20221006.15},
  eprint = {https://article.sciencepublishinggroup.com/pdf/10.11648.j.ajbio.20221006.15},
  abstract = {In the present investigation, in vivo effects of wasp toxin were evaluated on reversal of metabolic enzymes after providing purified anti-venom antibodies (anti-toxins) at 4 hour of treatment with 40% 24-h LD50. Venom glands of yellow wasp Polistes flavus were homogenized and loaded on gel filtration column for purification and isolation of venom toxins/proteins from wasp Polistes flavus. These proteins were venom proteins ranging from 14.3-63 kDa. The yellow wasp venom proteins obtained from the lyophilization of the two peaks caused toxicity in the albino mice. The LD50 of the yellow wasp Polistes flavus venom protein was found 36.11 mg/kilogram body weight i.e., 0.03611 mg/gram body weight of albino mice. Presence of antibodies in antiserum was tested by using the immune-double diffusion method of Ouchterlony (1962). A precipitin ring was obtained by filling purified antigen and antibody interaction after 24 hrs. Albino mice were treated with 40% of 24-h LD50 of purified wasp venom pre-incubated with different doses of purified wasp anti-venom and the neutralizing effects of anti-venom was measured in terms of reversal of metabolic alterations caused by wasp venom, after 4 hours of the treatment. The purified wasp anti-venom significantly (p<0.05) reversed the metabolic alterations caused by the wasp venom. The reversal of venom induced metabolic alteration in alkaline phosphatase, acid phosphatase, glutamate pyruvate transaminase, glutamate oxaloacetate transaminase, lactic dehydrogenase and acetylcholinesterase activity in the serum of albino mice was dose dependent (p<0.05, student t-test). This restoration of enzyme levels in blood serum, liver and gastrocnemius muscles of albino mice also display healing of liver damage, and necrosis in hepatic cells.},
 year = {2022}
}

Copy | Download

TY  - JOUR
T1  - Wasp Venom (Polistes flavus) Induced Bio-molecular and Enzymatic Alterations in Albino Mice and Its Reversal After Using Anti-venom
AU  - Krishna Kumar Prajapati
AU  - Ravi Kant Upadhyay
Y1  - 2022/12/23
PY  - 2022
N1  - https://doi.org/10.11648/j.ajbio.20221006.15
DO  - 10.11648/j.ajbio.20221006.15
T2  - American Journal of BioScience
JF  - American Journal of BioScience
JO  - American Journal of BioScience
SP  - 206
EP  - 219
PB  - Science Publishing Group
SN  - 2330-0167
UR  - https://doi.org/10.11648/j.ajbio.20221006.15
AB  - In the present investigation, in vivo effects of wasp toxin were evaluated on reversal of metabolic enzymes after providing purified anti-venom antibodies (anti-toxins) at 4 hour of treatment with 40% 24-h LD50. Venom glands of yellow wasp Polistes flavus were homogenized and loaded on gel filtration column for purification and isolation of venom toxins/proteins from wasp Polistes flavus. These proteins were venom proteins ranging from 14.3-63 kDa. The yellow wasp venom proteins obtained from the lyophilization of the two peaks caused toxicity in the albino mice. The LD50 of the yellow wasp Polistes flavus venom protein was found 36.11 mg/kilogram body weight i.e., 0.03611 mg/gram body weight of albino mice. Presence of antibodies in antiserum was tested by using the immune-double diffusion method of Ouchterlony (1962). A precipitin ring was obtained by filling purified antigen and antibody interaction after 24 hrs. Albino mice were treated with 40% of 24-h LD50 of purified wasp venom pre-incubated with different doses of purified wasp anti-venom and the neutralizing effects of anti-venom was measured in terms of reversal of metabolic alterations caused by wasp venom, after 4 hours of the treatment. The purified wasp anti-venom significantly (p<0.05) reversed the metabolic alterations caused by the wasp venom. The reversal of venom induced metabolic alteration in alkaline phosphatase, acid phosphatase, glutamate pyruvate transaminase, glutamate oxaloacetate transaminase, lactic dehydrogenase and acetylcholinesterase activity in the serum of albino mice was dose dependent (p<0.05, student t-test). This restoration of enzyme levels in blood serum, liver and gastrocnemius muscles of albino mice also display healing of liver damage, and necrosis in hepatic cells.
VL  - 10
IS  - 6
ER  -

Copy | Download

Author Information

Krishna Kumar Prajapati

Immune Biological Lab, Department of Zoology, Deen Dayal Upadhyaya Gorakhpur University, Gorakhpur, India
Ravi Kant Upadhyay

Immune Biological Lab, Department of Zoology, Deen Dayal Upadhyaya Gorakhpur University, Gorakhpur, India

Download PDF

Sections

Plain Text BibTeX RIS

APA Style

Krishna Kumar Prajapati, Ravi Kant Upadhyay. (2022). Wasp Venom (Polistes flavus) Induced Bio-molecular and Enzymatic Alterations in Albino Mice and Its Reversal After Using Anti-venom. American Journal of BioScience, 10(6), 206-219. https://doi.org/10.11648/j.ajbio.20221006.15

Copy | Download

ACS Style

Krishna Kumar Prajapati; Ravi Kant Upadhyay. Wasp Venom (Polistes flavus) Induced Bio-molecular and Enzymatic Alterations in Albino Mice and Its Reversal After Using Anti-venom. Am. J. BioScience 2022, 10(6), 206-219. doi: 10.11648/j.ajbio.20221006.15

Copy | Download

AMA Style

Krishna Kumar Prajapati, Ravi Kant Upadhyay. Wasp Venom (Polistes flavus) Induced Bio-molecular and Enzymatic Alterations in Albino Mice and Its Reversal After Using Anti-venom. Am J BioScience. 2022;10(6):206-219. doi: 10.11648/j.ajbio.20221006.15

Copy | Download

@article{10.11648/j.ajbio.20221006.15,
  author = {Krishna Kumar Prajapati and Ravi Kant Upadhyay},
  title = {Wasp Venom (Polistes flavus) Induced Bio-molecular and Enzymatic Alterations in Albino Mice and Its Reversal After Using Anti-venom},
  journal = {American Journal of BioScience},
  volume = {10},
  number = {6},
  pages = {206-219},
  doi = {10.11648/j.ajbio.20221006.15},
  url = {https://doi.org/10.11648/j.ajbio.20221006.15},
  eprint = {https://article.sciencepublishinggroup.com/pdf/10.11648.j.ajbio.20221006.15},
  abstract = {In the present investigation, in vivo effects of wasp toxin were evaluated on reversal of metabolic enzymes after providing purified anti-venom antibodies (anti-toxins) at 4 hour of treatment with 40% 24-h LD50. Venom glands of yellow wasp Polistes flavus were homogenized and loaded on gel filtration column for purification and isolation of venom toxins/proteins from wasp Polistes flavus. These proteins were venom proteins ranging from 14.3-63 kDa. The yellow wasp venom proteins obtained from the lyophilization of the two peaks caused toxicity in the albino mice. The LD50 of the yellow wasp Polistes flavus venom protein was found 36.11 mg/kilogram body weight i.e., 0.03611 mg/gram body weight of albino mice. Presence of antibodies in antiserum was tested by using the immune-double diffusion method of Ouchterlony (1962). A precipitin ring was obtained by filling purified antigen and antibody interaction after 24 hrs. Albino mice were treated with 40% of 24-h LD50 of purified wasp venom pre-incubated with different doses of purified wasp anti-venom and the neutralizing effects of anti-venom was measured in terms of reversal of metabolic alterations caused by wasp venom, after 4 hours of the treatment. The purified wasp anti-venom significantly (p<0.05) reversed the metabolic alterations caused by the wasp venom. The reversal of venom induced metabolic alteration in alkaline phosphatase, acid phosphatase, glutamate pyruvate transaminase, glutamate oxaloacetate transaminase, lactic dehydrogenase and acetylcholinesterase activity in the serum of albino mice was dose dependent (p<0.05, student t-test). This restoration of enzyme levels in blood serum, liver and gastrocnemius muscles of albino mice also display healing of liver damage, and necrosis in hepatic cells.},
 year = {2022}
}

Copy | Download

TY  - JOUR
T1  - Wasp Venom (Polistes flavus) Induced Bio-molecular and Enzymatic Alterations in Albino Mice and Its Reversal After Using Anti-venom
AU  - Krishna Kumar Prajapati
AU  - Ravi Kant Upadhyay
Y1  - 2022/12/23
PY  - 2022
N1  - https://doi.org/10.11648/j.ajbio.20221006.15
DO  - 10.11648/j.ajbio.20221006.15
T2  - American Journal of BioScience
JF  - American Journal of BioScience
JO  - American Journal of BioScience
SP  - 206
EP  - 219
PB  - Science Publishing Group
SN  - 2330-0167
UR  - https://doi.org/10.11648/j.ajbio.20221006.15
AB  - In the present investigation, in vivo effects of wasp toxin were evaluated on reversal of metabolic enzymes after providing purified anti-venom antibodies (anti-toxins) at 4 hour of treatment with 40% 24-h LD50. Venom glands of yellow wasp Polistes flavus were homogenized and loaded on gel filtration column for purification and isolation of venom toxins/proteins from wasp Polistes flavus. These proteins were venom proteins ranging from 14.3-63 kDa. The yellow wasp venom proteins obtained from the lyophilization of the two peaks caused toxicity in the albino mice. The LD50 of the yellow wasp Polistes flavus venom protein was found 36.11 mg/kilogram body weight i.e., 0.03611 mg/gram body weight of albino mice. Presence of antibodies in antiserum was tested by using the immune-double diffusion method of Ouchterlony (1962). A precipitin ring was obtained by filling purified antigen and antibody interaction after 24 hrs. Albino mice were treated with 40% of 24-h LD50 of purified wasp venom pre-incubated with different doses of purified wasp anti-venom and the neutralizing effects of anti-venom was measured in terms of reversal of metabolic alterations caused by wasp venom, after 4 hours of the treatment. The purified wasp anti-venom significantly (p<0.05) reversed the metabolic alterations caused by the wasp venom. The reversal of venom induced metabolic alteration in alkaline phosphatase, acid phosphatase, glutamate pyruvate transaminase, glutamate oxaloacetate transaminase, lactic dehydrogenase and acetylcholinesterase activity in the serum of albino mice was dose dependent (p<0.05, student t-test). This restoration of enzyme levels in blood serum, liver and gastrocnemius muscles of albino mice also display healing of liver damage, and necrosis in hepatic cells.
VL  - 10
IS  - 6
ER  -

Copy | Download