KINETIC PARAMETER ANALYSIS OF MYELOPEROXIDASE IN THE PRESENCE OF SOME COSUSBTRATES IN SALIVA OF NEWBORN AT RISK OF SEPSIS
Objective: During infection like sepsis, myeloperoxidase (MPO) enzyme will be generated from the neutrophil. This enzyme will catalyze the
oxidation of halide or pseudohalide (Cl, I-, SCN, and Br-) using hydrogen peroxide (H2O2). However, the mechanism by which oxidation of these several
cosubstrates in neonatal sepsis is unknown. Here, we have compared the kinetic parameter of MPO in saliva of newborn at risk of sepsis with or
without the presence of these several cosubstrates.
Methods: In this experiment, saliva samples were taken from newborn in health (n = 20) and risk of sepsis (n = 20). Saliva samples from each group
then homogenized and divided into four groups. Group 1 served as control which contains saliva+H2O2; Group 2 contains saliva+H2O2+Cl−; Group 3
contains saliva+H2O2+I−; and Group 4 contains saliva+H2O2+SCN−. After 1 h incubation, the kinetic parameters (Km and Vmax) were analyzed.
Results: The result shows that in sepsis condition, compared without the presence of some cosubstrates, it seems the addition of some cosubstrate
will increase the affinity between MPO, H2O2, and the cosubstrate. Between these three cosubstrates, it seems in sepsis condition MPO will oxidize Cl−.
Conclusion: In sepsis condition, MPO works by a common mechanism, that is, oxidizing Cl− to hypochlorous acid than another cosubstrate.
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