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Journal ArticleDOI: 10.1080/13813455.2019.1623265

Synthesis of novel tris-chalcones and determination of their inhibition profiles against some metabolic enzymes.

04 Mar 2021-Archives of Physiology and Biochemistry (Informa UK Limited)-Vol. 127, Iss: 2, pp 153-161
Abstract: In this study, we report the synthesis of novel tris-chalcones and testing of human carbonic anhydrase I, and II isoenzymes (hCA I, and hCA II), acetylcholinesterase (AChE), butyrylcholinesterase (...

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Topics: Carbonic Anhydrase I (72%), Carbonic anhydrase (58%), Butyrylcholinesterase (51%) ... read more

18 results found

Open access
01 Jan 2014-
Abstract: Sulphamides [1] and sulphonamides [2] are importantbiologically active compounds. In the last decades a lot ofsulphamide and sulphonamide drugs have appeared inthe markets. Quinagolide (1), a dopaminergic drug, isan antihyperprolactinemia agent [3]. Compound 2 (JNJ-26990990) has potential use in the treatment of depression,neuropathic and inflammatory pains [4]. The sulphonamidedrug sultiame (3) is an anticonvulsant used in the treatmentof epilepsy and West syndrome [5]. Acetazolamide (AZA, 4), adrug alsoknownas carbonicanhydrase (CA) inhibitor,isusedin the treatment of glaucoma [6] and idiopathic intracranialhypertension [7] (Figure 1).CA (E.C.: is a protein that is well suited to serve as amodel in many types of biophysical, bioanalytical andphysical-organic chemical studies as well as for inhibitordrug design studies. This enzyme catalyses the hydration ofcarbon dioxide (CO

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91 Citations

Open accessJournal ArticleDOI: 10.1080/10942912.2019.1656232
İlhami Gülçin1, Ruya Kaya2, Ahmet C. Gören3, Hulya Akincioglu2  +6 moreInstitutions (6)
Abstract: Ethanolic (EEC) and aqueous (WEC) extracts of cinnamon (Cinnamomum verum) were evaluated for their antioxidant profiles by eight distinguished bioanalytical antioxidant methods. Their inhibitory ef...

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Topics: Cinnamomum verum (68%)

38 Citations

Journal ArticleDOI: 10.1016/J.BCAB.2020.101711
Abstract: Some biochemical properties including phenolic content, anticholinergic, antidiabetic, and antioxidant activities of Stachys annua were determined in this study. The methanol extract of Stachys annua (MESA) and the water extract of Stachys annua (WESA) were prepared and used for all biochemical analyses. Antioxidant capacities of MESA and WESA were evaluated by six different in vitro bioanalytical methods including three reducing antioxidant methods and three radical scavenging antioxidant methods. Also, enzyme inhibition effect of Stachys annua against acetylcholinesterase (AChE), butyrylcholinesterase (BChE), α-amylase, and α-glycosidase enzymes were determined separately. According to the results, both extracts showed high inhibition effects against α-amylase and α-glycosidase enzymes, whereas they showed low inhibition effects against AChE and BChE enzymes. The IC50 values of MESA and WESA against AChE (119.8 ± 2.4 μg/mL and 150.1 ± 3.0 μg/mL), BChE (192.1 ± 3.8 μg/mL and 186.7 ± 3.7 μg/mL), α-glycosidase (25.7 ± 0.5 μg/mL and 18.7 ± 0.4 μg/mL), and α-amylase (43.3 ± 0.9 μg/mL and 11.4 ± 0.2 μg/mL) were determined, respectively. Another goal of the study was to evaluate the phenolic compositions of Stachys annua by liquid chromatography and tandem mass spectrometry (LC-MS/MS). Quercetagetin-3,6-dimethylether (178.6 ± 33.5 μg/g), chlorogenic acid (118.2 ± 16.4 μg/g), and fumaric acid (102.5 ± 7.1 μg/g) were identified as major compounds in MESA. On the other hand, fumaric acid (309.5 ± 21.5 μg/g), apigenin (144.6 ± 11.7 μg/g), and chlorogenic acid (78.1 ± 10.8 μg/g) were identified as major compounds in WESA. This study will be a scientific base for further studies about Stachys annua for food or medicinal utilization.

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Topics: Chlorogenic acid (52%)

29 Citations

Journal ArticleDOI: 10.1080/07391102.2020.1736631
Abstract: Carbonic anhydrases (CAs) are potent dehydration of carbonic acid and catalyst of the reversible hydration of carbon dioxide. Here, CA I and CA II was purified from human erythrocytes using the sim...

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Topics: Carbonic Anhydrase I (81%), Carbonic anhydrase (67%), Carbonic acid (61%)

26 Citations

Journal ArticleDOI: 10.1016/J.EJMECH.2019.112013
Xue-Tao Xu1, Deng Xuyang1, Jie Chen1, Qi-Ming Liang1  +10 moreInstitutions (3)
Abstract: In this study, two series of coumarin derivatives 5a∼i and 6a∼i were synthesized, and their inhibitory activity against α-glucosidase was determined. The results indicated that most of the synthesized derivatives exhibited prominent inhibitory activities against α-glucosidase. Among them, compounds 5a and 5b showed the strongest inhibition with the IC50 values of 19.64 μM and 12.98 μM, respectively. Enzyme kinetic studies of compounds 5a and 5b proved that their inhibition was reversible and a mixed type. The KI and KIS values of compound 5a were calculated to be 27.39 μM and 13.02 μM, respectively, and the corresponding values for compound 5b being 27.02 μM and 13.65 μM, respectively. The docking studies showed that compound 5b could be inserted into the active pocket of α-glucosidase and form hydrogen bonds with LYS293 to enhance the binding affinity.

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Topics: Docking (molecular) (51%), Coumarin (50%)

24 Citations


89 results found

Journal ArticleDOI: 10.1038/227680A0
Ulrich K. Laemmli1Institutions (1)
15 Aug 1970-Nature
Abstract: Using an improved method of gel electrophoresis, many hitherto unknown proteins have been found in bacteriophage T4 and some of these have been identified with specific gene products. Four major components of the head are cleaved during the process of assembly, apparently after the precursor proteins have assembled into some large intermediate structure.

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Topics: Bacteriophage T5 (61%), Head morphogenesis (59%), Gap junction assembly (57%) ... read more

229,303 Citations

Journal ArticleDOI: 10.1016/0003-2697(76)90527-3
Marion M. Bradford1Institutions (1)
Abstract: A protein determination method which involves the binding of Coomassie Brilliant Blue G-250 to protein is described. The binding of the dye to protein causes a shift in the absorption maximum of the dye from 465 to 595 nm, and it is the increase in absorption at 595 nm which is monitored. This assay is very reproducible and rapid with the dye binding process virtually complete in approximately 2 min with good color stability for 1 hr. There is little or no interference from cations such as sodium or potassium nor from carbohydrates such as sucrose. A small amount of color is developed in the presence of strongly alkaline buffering agents, but the assay may be run accurately by the use of proper buffer controls. The only components found to give excessive interfering color in the assay are relatively large amounts of detergents such as sodium dodecyl sulfate, Triton X-100, and commercial glassware detergents. Interference by small amounts of detergent may be eliminated by the use of proper controls.

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Topics: Bradford protein assay (59%), Lowry protein assay (55%), Spectrin binding (55%) ... read more

214,383 Citations

Open accessJournal Article
01 Jan 1970-Nature
Abstract: Using an improved method of gel electrophoresis, many hitherto unknown proteins have been found in bacteriophage T4 and some of these have been identified with specific gene products. Four major components of the head are cleaved during the process of assembly, apparently after the precursor proteins have assembled into some large intermediate structure.

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Topics: Cleavage (embryo) (57%)

203,017 Citations

Journal ArticleDOI: 10.1016/0006-2952(61)90145-9
Abstract: A photometric method for determining acetylcholinesterase activity of tissue extracts, homogenates, cell suspensions, etc., has been described. The enzyme activity is measured by following the increase of yellow color produced from thiocholine when it reacts with dithiobisnitrobenzoate ion. It is based on coupling of these reactions: The latter reaction is rapid and the assay is sensitive (i.e. a 10 μ1 sample of blood is adequate). The use of a recorder has been most helpful, but is not essential. The method has been used to study the enzyme in human erythrocytes and homogenates of rat brain, kidney, lungs, liver and muscle tissue. Kinetic constants determined by this system for erythrocyte eholinesterase are presented. The data obtained with acetylthiocholine as substrate are similar to those with acetylcholine.

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Topics: Aryl-acylamidase activity (54%), Thiocholine (53%), Acetylthiocholine (53%) ... read more

20,867 Citations

Journal ArticleDOI: 10.1021/JA01318A036
Abstract: On the basis of the assumed theory the rate of the observed reaction is directly proportional to the concentration of the enzyme-substrate compound, (ES), a t all values of the concentration of the substrate, (S). It is proportional to (S) only a t low values of (S). The numerical value of the dissociation constant is given by the substrate concentration a t half-maximum velocity, where (E:l = (ES). The equilibrium in equation 1 may be heterogeneous or homogeneous. Hitchcock'\" has pointed

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Topics: Dissociation constant (57%)

11,016 Citations