Characterization of the xanthine oxidase inhibitory activity of alk(en)yl phenols and related compounds

2018 ◽  
Vol 155 ◽  
pp. 100-106 ◽  
Author(s):  
Noriyoshi Masuoka ◽  
Isao Kubo
Keyword(s):  
Xanthine Oxidase ◽  
Inhibitory Activity ◽  
Related Compounds

scholarly journals Synthesis and biological profiling of novel isocoumarin derivatives and related compounds

2021 ◽  
pp. 25-25
Author(s):  
Milena Simic ◽  
Slavica Eric ◽  
Ivan Boric ◽  
Annamaria Lubelska ◽  
Gniewomir Latacz ◽  
...  
Keyword(s):  
Inhibitory Activity ◽  
Ames Test ◽  
The Other ◽  
Moderate Activity ◽  
Mutagenic Potential ◽  
Cyp Enzymes ◽  
Related Compounds

In continuation of our study of substituted isocoumarins a series of novel 3-azolyl isocoumarin and their thio derivatives including related lactone compounds was prepared and biologically profiled against C. albicans showing, in general, moderate activity with MIC values in range of 4-60 mg mL?1. Additional characterization of selected compounds was carried out by exploring their activity on CYP3A4 and CYP2D6 enzymes whilst experiments on mutagenicity were performed by AMES test. The representative isocoumarins 3b, 4a and 4b showed less inhibitory activity on CYP enzymes compared to the reference inhibitors, ketoconazole and quinidine. Compound 4a showed a higher mutagenic potential than the other two compounds. Further characterization included cytotoxicity profiling against normal MRC5 cells.

Screening of Hungarian mushrooms for xanthine-oxidase inhibitory activity

Planta Medica ◽  
2013 ◽  
Vol 79 (13) ◽  
Author(s):  
A Ványolós ◽  
O Orbán-Gyapai ◽  
T Támadi ◽  
J Hohmann
Keyword(s):  
Xanthine Oxidase ◽  
Inhibitory Activity

Polyphenols from Cyclopia genistoides and their xanthine oxidase inhibitory activity

Planta Medica ◽  
2015 ◽  
Vol 81 (16) ◽  
Author(s):  
O Roza ◽  
A Martins ◽  
J Hohmann ◽  
WC Lai ◽  
FR Chang ◽  
...  
Keyword(s):  
Xanthine Oxidase ◽  
Inhibitory Activity

Characterization of an Abnormal Antithrombin (Milano 2) with Defective Thrombin Binding

1986 ◽  
Vol 56 (03) ◽  
pp. 349-352 ◽  
Author(s):  
A Tripodi ◽  
A Krachmalnicoff ◽  
P M Mannucci
Keyword(s):  
Venous Thromboembolism ◽  
Active Site ◽  
Inhibitory Activity ◽  
Antithrombin Iii ◽  
Factor Xa ◽  
Molecular Defect ◽  
Affinity Adsorption ◽  
Italian Family ◽  
Crossed Immunoelectrophoresis

SummaryFour members of an Italian family (two with histories of venous thromboembolism) had a qualitative defect of antithrombin III reflected by normal antigen concentrations and halfnormal antithrombin activity with or without heparin. Anti-factor Xa activities were consistently borderline low (about 70% of normal). For the propositus’ plasma and serum the patterns of antithrombin III in crossed-immunoelectrophoresis with or without heparin were indistinguishable from those of normal plasma or serum. A normal affinity of antithrombin III for heparin was documented by heparin-sepharose chromatography. Affinity adsorption of the propositus’ plasma to human α-thrombin immobilized on sepharose beads revealed defective binding of the anti thrombin III to thrombin-sepharose. Hence the molecular defect of this variant appears to be at the active site responsible for binding and neutralizing thrombin, thus accounting for the low thrombin inhibitory activity.

scholarly journals Sulfation of vitamin D3-related compounds-identification and characterization of the responsible human cytosolic sulfotransferases

FEBS Letters ◽  
2017 ◽  
Vol 591 (16) ◽  
pp. 2417-2425 ◽  
Author(s):  
Katsuhisa Kurogi ◽  
Yoichi Sakakibara ◽  
Masahito Suiko ◽  
Ming-Cheh Liu
Keyword(s):  
Vitamin D3 ◽  
Related Compounds ◽  
Identification And Characterization

scholarly journals Evaluation of Enzyme Inhibitory Activity of Flavonoids by Polydopamine-Modified Hollow Fiber-Immobilized Xanthine Oxidase

Molecules ◽  
2021 ◽  
Vol 26 (13) ◽  
pp. 3931
Author(s):  
Cong-Peng Zhao ◽  
Guo-Ying Chen ◽  
Yuan Wang ◽  
Hua Chen ◽  
Jia-Wen Yu ◽  
...  
Keyword(s):  
Xanthine Oxidase ◽  
Hollow Fiber ◽  
Inhibitory Activity ◽  
Ph Value ◽  
Enzymatic Reaction ◽  
Amino Acid Residues ◽  
Reaction Conditions ◽  
Docking Analysis ◽  
Dopamine Concentration ◽  
Immobilization Time

In this study, a polydopamine (PDA)-modified hollow fiber-immobilized xanthine oxidase (XOD) was prepared for screening potential XOD inhibitors from flavonoids. Several parameters for the preparation of PDA-modified hollow fiber-immobilized XOD, including the dopamine concentration, modification time, XOD concentration and immobilization time, were optimized. The results show that the optimal conditions for immobilized XOD activity were a dopamine concentration of 2.0 mg/mL in 10.0 mM Tris-HCl buffer (pH 8.5), a modification time of 3.0 h, an XOD concentration of 1000 μg/mL in 10.0 mM phosphate buffer (pH 7.5) and an immobilization time of 3.0 h. Subsequently, the enzymatic reaction conditions such as the pH value and temperature were investigated, and the enzyme kinetics and inhibition parameters were determined. The results indicate that the optimal pH value (7.5) and temperature (37 °C) of the PDA-modified hollow fiber-immobilized XOD were consistent with the free enzyme. Moreover, the PDA-modified hollow fiber-immobilized XOD could still maintain above 50% of its initial immobilized enzyme activity after seven consecutive cycles. The Michaelis–Menten constant (Km) and the half-maximal inhibitory concentration (IC50) of allopurinol on the immobilized XOD were determined as 0.25 mM and 23.2 μM, respectively. Furthermore, the PDA-modified hollow fiber-immobilized XOD was successfully applied to evaluate the inhibitory activity of eight flavonoids. Quercetin, apigenin, puerarin and epigallocatechin showed a good inhibition effect, and their percentages of inhibition were (79.86 ± 3.50)%, (80.98 ± 0.64)%, (61.15 ± 6.26)% and (54.92 ± 0.41)%, respectively. Finally, molecular docking analysis further verified that these four active compounds could bind to the amino acid residues in the XOD active site. In summary, the PDA-modified hollow fiber-immobilized XOD is an efficient method for the primary screening of XOD inhibitors from natural products.

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