14 research outputs found

    Inhibition of serum antibodies against N-LDL and G-LDL binding by D-ribose (♦), N-LDL (▴) and G-LDL (▪) respectively.

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    <p>The microtiter plate was coated with D-ribose, N-LDL and G-LDL (10 µg/ml) respectively. Each data represents average of three experiments. The values represent the mean ± SD.</p

    Level of induced antibodies against D-ribose-modified LDL.

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    <p>Direct binding ELISA of D-ribose antisera (□), N-LDL antisera (▴), G-LDL antisera (♦) and preimmune sera (▪). The microtiter wells were coated with D-ribose, N-LDL and G-LDL (10 µg/ml) in direct binding ELISA of D-ribose antisera, native LDL antisera and G-LDL antisera respectively. Each data represents average of three experiments. The values represent the mean ± SD.</p

    Effect of CFA, D-ribose, N-LDL and G-LDL on plasma TBARS and Conjugated Diene (CD) in control and treated NZW female rabbits.

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    <p>Each data represents average of three experiments. The values represent the mean ± SD.</p><p>Effect of CFA, D-ribose, N-LDL and G-LDL on plasma TBARS and Conjugated Diene (CD) in control and treated NZW female rabbits.</p

    Molecular rationale delineating the role of lycopene as a potent HMG-CoA reductase inhibitor: <i>in vitro</i> and <i>in silico</i> study

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    <p>This study initially aimed to depict the molecular rationale evolving the role of lycopene in inhibiting the enzymatic activity of β-hydroxy-β-methylglutaryl-CoA (HMG-CoA) reductase via <i>in vitro</i> and <i>in silico</i> analysis. Our results illustrated that lycopene exhibited strong HMG-CoA reductase inhibitory activity (IC<sub>50</sub> value of 36 ng/ml) quite better than pravastatin (IC<sub>50</sub> = 42 ng/ml) and strong DPPH free radical scavenging activity (IC<sub>50</sub> value = 4.57 ± 0.23 μg/ml) as compared to ascorbic acid (IC<sub>50</sub> value = 9.82 ± 0.42 μg/ml). Moreover, the <i>K</i><sub><i>i</i></sub> value of lycopene (36 ng/ml) depicted via Dixon plot was well concurred with an IC<sub>50</sub> value of 36 ± 1.8 ng/ml. Moreover, molecular informatics study showed that lycopene exhibited binding energy of −5.62 kcal/mol indicating high affinity for HMG-CoA reductase than HMG-CoA (Δ<i>G</i>: −5.34 kcal/mol). Thus, <i>in silico</i> data clearly demonstrate and support the <i>in vitro</i> results that lycopene competitively inhibit HMG-CoA reductase activity by binding at the hydrophobic portion of HMG-CoA reductase.</p

    Hemoglobin-δ-gluconolactone assay.

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    <p>Results are mean ±SD and were compared with untreated blood (A = control blood; B = blood+δ-glu; C = blood+δ-glu+10 mM AG; D = blood+δ-glu+10 µM MF; E = blood+δ-glu+100 µM MF; F = blood+δ-glu+500 µM MF; G = blood+ δ-glu+1 mM MF; H = blood+ δ-glu+1 mM PM; I = blood+ δ-glu+5 mM PM; J = blood+ δ-glu+10 mM PM and K = blood+δ-glu+20 mM PM). The various groups are significantly different (p<0.01) from the other.</p
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