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Efficacy of Silene arenosa extract on acetylcholinesterase in Bungarus sindanus (krait) venom.
Shah, Adil; Ahmed, Mushtaq; Sher, Naila; Mushtaq, Nadia; Khan, Rahmat-Ali.
  • Shah A; Department of Biotechnology, Faculty of Biological Sciences, University of Science & Technology, Bannu 28100, KPK-Pakistan.
  • Ahmed M; Department of Biotechnology, Faculty of Biological Sciences, University of Science & Technology, Bannu 28100, KPK-Pakistan.
  • Sher N; Department of Biotechnology, Faculty of Biological Sciences, University of Science & Technology, Bannu 28100, KPK-Pakistan.
  • Mushtaq N; Department of Botany, Faculty of Biological Sciences, University of Science & Technology, Bannu 28100, KPK-Pakistan.
  • Khan RA; Department of Biotechnology, Faculty of Biological Sciences, University of Science & Technology, Bannu 28100, KPK-Pakistan.
  • Fozia; Department of Biochemistry, KMU Institute of Medical Sciences, Kohat 26000, Pakistan.
  • Midrarullah; Department of Biotechnology, Saheed Benazir Bhutto University, Sheringal, Dir Upper, KPK-Pakistan.
J Tradit Chin Med ; 41(3): 349-354, 2021 06.
Article in English | MEDLINE | ID: covidwho-1357700
ABSTRACT

OBJECTIVE:

To examine the efficacy of Silene arenosa extract on acetylcholinesterase (AChE) of krait (Bungarus Sindanus) snake venom.

METHODS:

The present project designed to evaluate the inhibition of AChE by following standard procedures.

RESULTS:

Statistical analysis of the results showed that Silene arenosa exerted 73% inhibition against the krait venom acetylcholinesterase at fixed substrate acetylcholine (ACh) concentration (0.5 mM). Kinetic analysis using the Lineweaver Burk plot revealed that Silene arenosa caused a competitive type of inhibition i.e. Km values increased from 26.6 to 93.3 mM (26.6% to 93.3%) and Vmax remained constant in a concentration-dependent manner. Silene arenosa competes with the substrate to bind at the active site of the enzyme. The Kmapp of venom AChE for Silene arenosa increased from 60% to 81.6% and the Vmaxapp remains constant. Ki (inhibition constant was estimated to be 48 µg for snake venom; while the Km (Michaelis-Menten constant of AChE- substrate into AChE and product) was estimated to be 0.5 mM. The IC50 of AchE calculated for Silene arenosa was 67 µg.

CONCLUSION:

The present results suggest that Silene arenosa extract can be considered as an inhibitor of snake venom AChE.
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Full text: Available Collection: International databases Database: MEDLINE Main subject: Acetylcholinesterase / Silene Type of study: Experimental Studies Limits: Animals / Humans Language: English Journal: J Tradit Chin Med Year: 2021 Document Type: Article

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Full text: Available Collection: International databases Database: MEDLINE Main subject: Acetylcholinesterase / Silene Type of study: Experimental Studies Limits: Animals / Humans Language: English Journal: J Tradit Chin Med Year: 2021 Document Type: Article