Trypanocidal efficacy of two indigeneous ethanolic plant extracts (Mimosa pigra and Ipomoea asarifolia) against Trypanosoma evansi phospholipase A2 activity
Objective: To study the inhibitory activity of ethanolic extract from Mimosa pigra and Ipomoea asarifolia against Trypanosoma evansi (T. evansi) calcium dependent phospholipase A2. Methods: The calcium dependent phospholipase A2 (E C 3.1.1.4) enzyme was isolated from T. evansi and purified to electr...
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Format: | Article |
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Wolters Kluwer Medknow Publications
2015-03-01
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Series: | Journal of Acute Disease |
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Online Access: | http://www.sciencedirect.com/science/article/pii/S2221618914600780 |
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author | Yusuf Alkali A.K. Gana A Abdulkadir Nzelibe C. Humphrey |
author_facet | Yusuf Alkali A.K. Gana A Abdulkadir Nzelibe C. Humphrey |
author_sort | Yusuf Alkali |
collection | DOAJ |
description | Objective: To study the inhibitory activity of ethanolic extract from Mimosa pigra and Ipomoea asarifolia against Trypanosoma evansi (T. evansi) calcium dependent phospholipase A2.
Methods: The calcium dependent phospholipase A2 (E C 3.1.1.4) enzyme was isolated from T. evansi and purified to electrophoretic homogeneity under non denaturing conditions. It was solubilized from T. evansi cells recovered from white albino rats which were previously inoculated by intraperitoneal injection of infected camel blood. Two indigeneous ethanolic plant extracts used locally for treatment of trypanosomiasis were tested for the inhibition of phospholipases A2.
Results: Double reciprocal plots of the initial velocity data of the inhibition by the indigenous plant extracts revealed a noncompetitive pattern of inhibition for the Ipomoea asarifolia and a competitive inhibition for Mimosa pigra in a dose dependent fashion. The extrapolated inhibition binding constant (Ki) of these extracts were found to be 2.0×102 μg/mL and 1.12×102 μg/mL respectively.
Conclusions: The low Ki values obtained for these extracts towards this enzyme are an indication of high affinity of the extract or the active components (present in the plants) are for these enzyme and therefore, could be explored to serve as a cheap source of T. evansi PLA2 antidote and as well help in designing a novel drug with high efficiency. |
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issn | 2221-6189 |
language | English |
last_indexed | 2024-12-19T16:31:17Z |
publishDate | 2015-03-01 |
publisher | Wolters Kluwer Medknow Publications |
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series | Journal of Acute Disease |
spelling | doaj.art-ec1009ef3ce34eeb84313218972ff3322022-12-21T20:14:10ZengWolters Kluwer Medknow PublicationsJournal of Acute Disease2221-61892015-03-0141283110.1016/S2221-6189(14)60078-0Trypanocidal efficacy of two indigeneous ethanolic plant extracts (Mimosa pigra and Ipomoea asarifolia) against Trypanosoma evansi phospholipase A2 activityYusuf Alkali0A.K. Gana1A Abdulkadir2Nzelibe C. Humphrey3national Cereal Research Institute Badeggi-Bida, Nigerianational Cereal Research Institute Badeggi-Bida, NigeriaFederal University of Technology Minna, NigeriaDepartment of Biochemistry, Ahmadu Bello University, Zaria, NigeriaObjective: To study the inhibitory activity of ethanolic extract from Mimosa pigra and Ipomoea asarifolia against Trypanosoma evansi (T. evansi) calcium dependent phospholipase A2. Methods: The calcium dependent phospholipase A2 (E C 3.1.1.4) enzyme was isolated from T. evansi and purified to electrophoretic homogeneity under non denaturing conditions. It was solubilized from T. evansi cells recovered from white albino rats which were previously inoculated by intraperitoneal injection of infected camel blood. Two indigeneous ethanolic plant extracts used locally for treatment of trypanosomiasis were tested for the inhibition of phospholipases A2. Results: Double reciprocal plots of the initial velocity data of the inhibition by the indigenous plant extracts revealed a noncompetitive pattern of inhibition for the Ipomoea asarifolia and a competitive inhibition for Mimosa pigra in a dose dependent fashion. The extrapolated inhibition binding constant (Ki) of these extracts were found to be 2.0×102 μg/mL and 1.12×102 μg/mL respectively. Conclusions: The low Ki values obtained for these extracts towards this enzyme are an indication of high affinity of the extract or the active components (present in the plants) are for these enzyme and therefore, could be explored to serve as a cheap source of T. evansi PLA2 antidote and as well help in designing a novel drug with high efficiency.http://www.sciencedirect.com/science/article/pii/S2221618914600780Phospholipase A2Indigeneous plant extractTrypanosomiasis |
spellingShingle | Yusuf Alkali A.K. Gana A Abdulkadir Nzelibe C. Humphrey Trypanocidal efficacy of two indigeneous ethanolic plant extracts (Mimosa pigra and Ipomoea asarifolia) against Trypanosoma evansi phospholipase A2 activity Journal of Acute Disease Phospholipase A2 Indigeneous plant extract Trypanosomiasis |
title | Trypanocidal efficacy of two indigeneous ethanolic plant extracts (Mimosa pigra and Ipomoea asarifolia) against Trypanosoma evansi phospholipase A2 activity |
title_full | Trypanocidal efficacy of two indigeneous ethanolic plant extracts (Mimosa pigra and Ipomoea asarifolia) against Trypanosoma evansi phospholipase A2 activity |
title_fullStr | Trypanocidal efficacy of two indigeneous ethanolic plant extracts (Mimosa pigra and Ipomoea asarifolia) against Trypanosoma evansi phospholipase A2 activity |
title_full_unstemmed | Trypanocidal efficacy of two indigeneous ethanolic plant extracts (Mimosa pigra and Ipomoea asarifolia) against Trypanosoma evansi phospholipase A2 activity |
title_short | Trypanocidal efficacy of two indigeneous ethanolic plant extracts (Mimosa pigra and Ipomoea asarifolia) against Trypanosoma evansi phospholipase A2 activity |
title_sort | trypanocidal efficacy of two indigeneous ethanolic plant extracts mimosa pigra and ipomoea asarifolia against trypanosoma evansi phospholipase a2 activity |
topic | Phospholipase A2 Indigeneous plant extract Trypanosomiasis |
url | http://www.sciencedirect.com/science/article/pii/S2221618914600780 |
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