Study on the activity difference of macromonomers for preparing polycarboxylic superplasticizers

2020 ◽  
Vol 137 (26) ◽  
pp. 48844 ◽  
Author(s):  
Guanjie Liu ◽  
Xuehong Wei ◽  
Ziwei Wang ◽  
Jianguo Ren
Keyword(s):  
Activity Difference

Shelf Life and Moisture Transfer Predictions in a Composite Food Product: Impact of Preservation Techniques

2008 ◽  
Vol 4 (4) ◽  
Author(s):  
Elisabeth Roca ◽  
Dorothée Adeline ◽  
Valérie Guillard ◽  
Stéphane Guilbert ◽  
Nathalie Gontard
Keyword(s):  
Shelf Life ◽  
Water Activity ◽  
Food System ◽  
Moisture Transfer ◽  
Food Product ◽  
Moisture Diffusivity ◽  
Point Of View ◽  
Effective Moisture Diffusivity ◽  
Effective Moisture ◽  
Activity Difference

Three techniques to prevent moisture transfer in a multidomain food system constituted by a cookie in contact with a moist filling were investigated: reducing the water activity difference between components, reducing the effective moisture diffusivity of the cereal-based component, and applying an edible moisture barrier at the interface between components. Shelf-life of the food product was extended by 6 days by decreasing the water activity of the moist filling in contact from 0.99 to 0.64 (cookie aw being 0.23, 20°C). Decreasing effective moisture diffusivity from 1.56 to 0.99*10-11 m²/s by the addition of 2.35 g of fat in the formulation of the cookie was limited by technological and organoleptic considerations and allowed an extension of shelf-life of 2 more days. From a technical and nutritional point of view, the application of a sprayed edible barrier at the surface of the cookie was the more effective solution increasing shelf life of almost 8 days for only 1.7 g of fat per cookie.

Azobenzene-benzoylphenylureas as photoswitchable chitin synthesis inhibitors

2017 ◽  
Vol 15 (15) ◽  
pp. 3320-3323 ◽  
Author(s):  
Xue Tian ◽  
Chao Zhang ◽  
Qi Xu ◽  
Zhong Li ◽  
Xusheng Shao
Keyword(s):  
Uv Light ◽  
Chitin Synthesis ◽  
Mythimna Separata ◽  
Chitin Synthesis Inhibitors ◽  
Activity Difference

A prepared azobenzene-benzoylphenylurea can be activated upon irradiation with UV light, and shows 6-fold activity difference to armyworm (Mythimna separata) receptors.

scholarly journals Activity Landscape and Molecular Modeling to Explore the SAR of Dual Epigenetic Inhibitors: A Focus on G9a and DNMT1

2018 ◽  
Author(s):  
Edgar López-López ◽  
Fernando D. Prieto-Martínez ◽  
José L. Medina-Franco
Keyword(s):  
Data Set ◽  
Structure Activity ◽  
Activity Difference ◽  
Dual Inhibitors ◽  
Structure Similarity ◽  
Dynamics Simulations ◽  
Key Residues ◽  
High Structure ◽  
Molecular Docking And Dynamics ◽  
Activity Cliffs

In this work we discuss the insights from activity landscape, docking and molecular dynamics towards the understanding of the structure-activity relationships of dual inhibitors of major epigenetic targets: lysine metiltransferase (G9a) and DNA metiltranferase 1 (DNMT1). The study was based on a novel data set of 50 published compounds with reported experimental activity for both targets. The activity landscape analysis revealed the presence of activity cliffs, e.g., pairs of compounds with high structure similarity but large activity difference. Activity cliffs were further rationalized at the molecular level by means of molecular docking and dynamics simulations that led to the identification of interactions with key residues involved in the dual activity or selectivity with the epigenetic targets.

Residual iodine on in-situ transformed bismuth nanosheets induced activity difference in CO2 electroreduction

2022 ◽  
Vol 55 ◽  
pp. 101802
Author(s):  
Dan Wang ◽  
Yanying Wang ◽  
Kuan Chang ◽  
Yaning Zhang ◽  
Zhenlin Wang ◽  
...  
Keyword(s):  
Co2 Electroreduction ◽  
Activity Difference

Activity landscape modeling of PPAR ligands with dual-activity difference maps

2012 ◽  
Vol 20 (11) ◽  
pp. 3523-3532 ◽  
Author(s):  
Oscar Méndez-Lucio ◽  
Jaime Pérez-Villanueva ◽  
Rafael Castillo ◽  
José L. Medina-Franco
Keyword(s):  
Landscape Modeling ◽  
Activity Difference ◽  
Ppar Ligands

Molecular-Level Understanding of the Photocatalytic Activity Difference between Anatase and Rutile Nanoparticles

2014 ◽  
Vol 126 (51) ◽  
pp. 14260-14265 ◽  
Author(s):  
Wooyul Kim ◽  
Takashi Tachikawa ◽  
Gun-hee Moon ◽  
Tetsuro Majima ◽  
Wonyong Choi
Keyword(s):  
Photocatalytic Activity ◽  
Molecular Level ◽  
Activity Difference

Ecto-Phosphatase Activities on the Cell Surface of the Amastigote Forms of Trypanosoma cruzi

1999 ◽  
Vol 54 (11) ◽  
pp. 977-984 ◽  
Author(s):  
José Roberto Meyer-Fernandes ◽  
Mario Alberto da Silva-Neto ◽  
Mirna dos Santos Soares ◽  
Eloise Fernandes ◽  
Anibal Eugênio Vercesi ◽  
...  
Keyword(s):  
Amino Acids ◽  
Cell Surface ◽  
Trypanosoma Cruzi ◽  
Phosphatase Activity ◽  
Sodium Fluoride ◽  
Competitive Inhibitor ◽  
Physiological Conditions ◽  
Basal Activity ◽  
Activity Difference ◽  
Pnpp Hydrolysis

Abstract Live Trypanosoma cruzi amastigotes hydrolyzed p-nitrophenylphosphate (PNPP), phos-pho-amino-acids and 32P-casein under physiologically appropriate conditions. PNPP was hy­drolysed at a rate of 80 nmol ·mg -1 ·h -1 in the presence of 5 mм MgCl2, pH 7.2 at 30 °C. In the absence of Mg2+ the activity was reduced 40% and we call this basal activity. At saturating concentration of PNPP, half-maximal PNPP hydrolysis was obtained with 0.22 mм MgCl2· Ca2+ had no effect on the basal activity, could not substitute Mg2+ as an activator and in contrast inhibited the PNPP hydrolysis stimulated by Mg2+ (I50 = 0.43 mм ) . In the absence of Mg2+ (basal activity) the stimulating half concentration (S0. 5) for PNPP was 1.57 mм , while at saturating MgCl2 concentrations the corresponding S0.5 for PNPP for Mg2+-stimulated phosphatase activity (difference between total minus basal phosphatase activity) was 0.99 mм . The Mg-dependent PNPP hydrolysis was strongly inhibited by sodium fluoride (NaF), vanadate and Zn2+ but not by tartrate and levamizole. The Mg-independent basal phosphatase activity was insensitive to tartrate, levamizole as well NaF and less inhibited by vanadate and Zn2+. Intact amastigotes were also able to hydrolyse phosphoserine, phos-phothreonine and phosphotyrosine but only the phosphotyrosine hydrolysis was stimulated by MgCl2 and inhibited by CaCl2 and phosphotyrosine was a competitive inhibitor of the PNPP hydrolysis stimulated by Mg2+. The cells were also able to hydrolyse 32P-casein phosphorylated on serine and threonine residues but only in the presence of MgCl2. These results indicate that in the amastigote form of T. cruzi there are at least two ectophosphatase activities, one of which is Mg2+ dependent and can dephosphorylate phospho-aminoacids and phosphoproteins under physiological conditions.

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