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Articles by A.B. Sallau
Total Records ( 2 ) for A.B. Sallau
  M.A. Ibrahim , A.B. Sallau , A. Salihu and K.C. Onwube
  Phospholipase A2 (EC. 3.1.1.4) was isolated and partially characterized from the erythrocytic stage of Plasmodium berghei (NK-65) obtained from experimentally infected mice with the objective of studying its kinetic properties and its possible role in the pathogenesis of malaria. The parasite collected by sucrose gradient centrifugation was subjected to lysis to obtain the crude phospholipase A2 which was assayed and subjected to some biochemical characterizations . The enzyme had broad pH and temperature ranges with optima of 7.5 and 37°C, respectively. Initial velocity studies for the determination of kinetic parameters with L-α lecithin as substrate revealed a KM and VMAX of 0.68 mg mL-1 and 52.60 μmol min-1, respectively. The P. berghei PLA2 was slightly activated by Ca2+ while Cu2+, Zn2+and Mn2+ were inhibitory to the enzyme. However, no enzyme activity was detected in the presence of Mg2+ and Hg2+. Considering the findings of this work, P. berghei can be said to contain PLA2 which has similar properties with some other parasites PLA2 and could be involved in cellular invasion and/or aneamia development during cerebral malaria.
  A.B. Sallau , G.C. Njoku , A.R. Olabisi , A.U. Wurochekke , A.A. Abdulkadir , Shehu Isah , M.S. Abubakar and S. Ibrahim
  Aqueous extract of Guiera senegalensis leaves was investigated for the inhibitory action on the activity of crude phospholipase and metalloprotease enzymes from Echis carinatus venom. Both enzymes were inhibited by the extract in a dose dependent fashion. Double reciprocal plots of the initial velocity data of the inhibition by the extract revealed a non-competitive pattern of inhibition for the metalloprotease and a competitive one for the phospholipase. Extrapolated Ki values were found to be 11.9 and 90 μg mL-1 for the metalloprotease and phospholipase, respectively.
 
 
 
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