Acetylcholinesterase activity of Ocimum Sanctum leaf extract
Abstract
Introduction: Ocimum sanctum leaf being an herb for all reasons, is multifunctional and a highly used herb for curing many ailments. Acetylcholinesterase is an enzyme produced in our bodies that is a primary cholinesterase and is mainly found in the neuromuscular junctions and junctions of chemical synapses of the cholinergic type. Its primary activity in such sites is to inhibit/terminate synaptic transmission. This study was performed so as to observe and evaluate the acetylcholinesterase activity of Ocimum sanctum leaf at various concentrations. On performing this study, we will be able to evaluate how potent Ocimum sanctum leaf extract is in inhibiting the enzyme Acetylcholinesterase. Materials and Methods: Ocimum sanctum extract was examined for their AchE inhibitory by the spectrophotometric method developed by Ellman et al, activities at different concentrations (5, 10, 20, 40, 80, 160 and 320 micrograms/ml) and were dissolved in a base- tris (0.05 M) buffer, following the spectrophotometric method. Results: Different concentrations of Ocimum sanctum extract were evaluated for the inhibitory effect on the activity of acetylcholinesterase. The plant extract exhibited potent inhibition of the ACh. The IC50 was found to be 54.57µg/ml. Maximum inhibition was found to be 83.16% at 320µg/ml. Conclusions: On performing the in vitro study, it was found that the ethanolic extract of Ocimum sanctum was a potent inhibitor of acetycholinesterase and therefore acts as an anticholinergic agent. Thus, giving scope for more revolutionary breakthroughs in the field of pharmacological actions of various plant extracts.
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