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• W2023372842 abstract "We purified a protein from the dromedary small intestine that displayed potent bactericidal activity against Gram-positive bacteria, and identified it as group-IIA phospholipase A₂ (DrPLA₂-IIA) by NH₂-terminal sequencing and enzymatic measurements. In fact, our findings revealed that the purified PLA₂-IIA was a monomeric protein with a molecular mass of about 14 kDa. Pure enzyme has a specific activity of 329 ± 25 U/mg at optimal conditions (pH 9.5 and 45 °C) in the presence of 6 mM NaDC and 7 mM CaCl₂ with egg yolk emulsion as substrate and binds with a higher affinity to PE than PS and PC. Furthermore, the DrPLA2-IIA activity was dependent on Ca(2+); other cations (Cd(2+), Co(2+), Fe(2+), Mg(2+), Mn(2+), and Zn(2+)) reduced the enzymatic activity notably, suggesting that the arrangement of the catalytic site presents an exclusive structure for Ca(2+). On the other hand, DrPLA2-IIA was highly bactericidal against Gram-positive bacteria with inhibition zones and IC₅₀ values in the range of 21-27 mm and 3.7-8 μg/ml, respectively, whereas Gram-negative bacteria exhibited a much higher resistance. These observations suggest that the main physiological role of DrPLA2-IIA could be the defense of the intestine against bacterial infections." @default.
• W2023372842 created "2016-06-24" @default.
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• W2023372842 date "2013-06-01" @default.
• W2023372842 modified "2023-10-16" @default.
• W2023372842 title "Purification, characterization and bactericidal activities of phospholipase A2 from the dromedary intestine" @default.
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• W2023372842 doi "https://doi.org/10.1016/j.ijbiomac.2013.03.020" @default.
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