Displaying all 2 publications

Abstract:
Sort:
  1. Abubakar M. Umar, Tham, Lik Gin, Natarajan Perumal, Nur Adeela Yasid, Hassan Mohd Daud, Mohd Yunus Shukor
    MyJurnal
    Acetylcholinesterase (AChE) is usually used as an inhibitive assay for insecticides. A lesserknown
    property of AChE is its inhibition by heavy metals. In this work, we evaluate an AChE
    from brains of Clarias batrachus (catfish) exposed to wastes from aquaculture industry as an
    inhibitive assay for heavy metals. We discovered that the AChE was inhibited completely by
    Hg2+, Ag2+, Pb2+, Cu2+, Cd2+, Cr6+ and Zn2+ during initial screening. When tested at various
    concentrations, the heavy metals exhibited exponential decay type inhibition curves. The
    calculated IC50 (mg/L) for the heavy metals Ag2+, Cu2+, Hg2+, Cr6+ and Cd2+ were 0.088, 0.078,
    0.071, 0.87 and 0.913, respectively. The IC50 for these heavy metals are comparable, and some
    are lower than the IC50 values from the cholinesterases from previously studied fish. The assay
    can be carried out in less than 30 minutes at ambient temperature.
  2. Abubakar M. Umar, Tham, Lik Gin, Natarajan Perumal, Nur A. Yasid, Hassan Mohd Daud, Mohd Y. Shukor
    MyJurnal
    In this work we assess the potential of acetylcholinesterase (AChE) from Oreochromis
    mossambicus (Toman) as a sensitive test for the presence of insecticides. The partial purification
    and characterization of a soluble AChE from Oreochromis mossambicus brain tissues using
    affinity chromatography gel (procainamide–Sephacryl S-1000) showed that the partially purified
    AChE was most active on acetylthiocholine (ATC) but had low activities on
    propionylthiocholine (PTC) and butyrylthiocholine (BTC), indicating that the partially purified
    fraction was predominantly AChE. Soluble AChE was partially purified 9.27-fold with a 91.12%
    yield. The partially purified AChE displayed the highest activity on ATC at pH 7 and at 30oC
    using 0.1 M Tris buffer. The enzyme exhibited Michaelis-Menten kinetic constants, Km, for
    ATC, BTC and PTC at 36, 77 and 250 μM, respectively, and the maximum velocities, Vmax, were
    18.75, 0.12 and 0.05 μmol/min/mg protein, respectively. Moreover, the AChE from
    Oreochromis mossambicus presented comparable sensitivity to carbamates and
    organophosphates insecticides than that from Electrophorus electricus and many other fish
    AChE by comparing half maximal inhibitory concentration values. Therefore, the enzyme is a
    valuable source for insecticides detection in Malaysian waters at lower cost.
Related Terms
Filters
Contact Us

Please provide feedback to Administrator (afdal@afpm.org.my)

External Links