pH-Dependent Transformation of Ag Nanoparticles in Anaerobic Processes

2013 ◽  
Vol 47 (22) ◽  
pp. 12630-12631 ◽  
Author(s):  
Ze-hua Liu ◽  
Yan Zhou ◽  
Abdul Majid Maszenan ◽  
Wun Jern Ng ◽  
Yu Liu
Keyword(s):  
Ag Nanoparticles ◽  
Anaerobic Processes ◽  
Ph Dependent

scholarly journals The pH-Dependent Stucture and Properties of Au and Ag Nanoparticles Produced by Tryptophan Reduction

2016 ◽  
Vol 11 (1) ◽  
Author(s):  
Iuliia Mukha ◽  
Nadiia Vityuk ◽  
Olga Severynovska ◽  
Anna Eremenko ◽  
Nataliia Smirnova
Keyword(s):  
Ag Nanoparticles ◽  
Ph Dependent

Mechanisms of the pH dependent generation of hydroxyl radicals and oxygen induced by Ag nanoparticles

Biomaterials ◽  
2012 ◽  
Vol 33 (30) ◽  
pp. 7547-7555 ◽  
Author(s):  
Weiwei He ◽  
Yu-Ting Zhou ◽  
Wayne G. Wamer ◽  
Mary D. Boudreau ◽  
Jun-Jie Yin
Keyword(s):  
Hydroxyl Radicals ◽  
Ag Nanoparticles ◽  
Ph Dependent

Correction to pH-Dependent Transformation of Ag Naoparticles in Anaerobic Processes

2014 ◽  
pp. 140128165313009
Author(s):  
Ze-hua Liu ◽  
Yan Zhou ◽  
Abdul Majid Maszenan ◽  
Wun Jern Ng ◽  
Yu Liu
Keyword(s):  
Anaerobic Processes ◽  
Ph Dependent

The Reaction of Thiol Compounds with the Vitamin-K Dependent Clotting Factors

1969 ◽  
Vol 21 (03) ◽  
pp. 573-579 ◽  
Author(s):  
P Fantl
Keyword(s):  
Prothrombin Time ◽  
Vitamin K ◽  
Anaerobic Conditions ◽  
Clotting Factors ◽  
Thiol Compounds ◽  
Aerobic Conditions ◽  
One Stage ◽  
Factor Ii ◽  
Ph Dependent ◽  
The One

SummaryTreatment of human and dog oxalated plasma with 0.2 to 1.0 × 10−1 M 2.3-dithiopropanol (BAL) or dithiothreitol (DTT) at 2–4° C for 30 min results in the reduction of the vitamin-K dependent clotting factors II, VII, IX and X to the respective-SH derivatives. The reaction is pH dependent. Under aerobic conditions the delayed one stage prothrombin time can be partly reversed. Under anaerobic conditions a gradual prolongation of the one stage prothrombin time occurs without reversal.In very diluted plasma treated with the dithiols, prothrombin can be converted into thrombin if serum as source of active factors VII and X is added. In contrast SH factors VII, IX and X are inactive in the specific tests. Reoxidation to active factors II, VII, IX and X takes place during adsorption and elution of the SH derivatives. The experiments have indicated that not only factor II but also factors VII, IX and X have active-S-S-centres.

Hydrothermal preparation of TiO2-Ag nanoparticles and its antimicrobial performance against human pathogenic microbial cells in water

BIOCELL ◽  
2018 ◽  
Vol 42 (3) ◽  
pp. 93-97 ◽  
Author(s):  
Mahmoud MOUSTAFA ◽  
Saad ALAMRI ◽  
Mohamed ELNOUBY ◽  
Tarek TAHA ◽  
M. A. ABU-SAIED ◽  
...  
Keyword(s):  
Ag Nanoparticles ◽  
Hydrothermal Preparation ◽  
Microbial Cells ◽  
Antimicrobial Performance

A Biological Approach of Silver (Ag) Nanoparticles Synthesis Using Leaf Extract of Adhatoda Vasica

2012 ◽  
Vol 3 (2) ◽  
pp. 177-179
Author(s):  
Dr. K.Vinoth Kumar Dr. K.Vinoth Kumar ◽  
◽  
Dr. C. Udayasoorian Dr. C. Udayasoorian
Keyword(s):  
Ag Nanoparticles ◽  
Leaf Extract ◽  
Adhatoda Vasica ◽  
Biological Approach ◽  
Nanoparticles Synthesis

Rationalizing the pH-Activity Response for Escherichia Coli’s Glycinamide Ribonucleotidetransformylase Through Computational Methods

2019 ◽  
Author(s):  
Adrian Roitberg ◽  
Pancham Lal Gupta
Keyword(s):  
Transfer Reaction ◽  
Catalytic Mechanism ◽  
Ph Dependence ◽  
Ph Effects ◽  
Dependent Manner ◽  
E Coli ◽  
Gar Tfase ◽  
Activity Curve ◽  
Ph Dependent ◽  
Formyl Transfer

<div>Human Glycinamide ribonucleotide transformylase (GAR Tfase), a regulatory enzyme in the de novo purine biosynthesis pathway, has been established as an anti-cancer target. GAR Tfase catalyzes the formyl transfer reaction from the folate cofactor to the GAR ligand. In the present work, we study E. coli GAR Tfase, which has high sequence similarity with the human GAR Tfase with most functional residues conserved. E. coli GAR Tfase exhibits structural changes and the binding of ligands that varies with pH which leads to change the rate of the formyl transfer reaction in a pH-dependent manner. Thus, the inclusion of pH becomes essential for the study of its catalytic mechanism. Experimentally, the pH-dependence of the kinetic parameter kcat is measured to evaluate the pH-range of enzymatic activity. However, insufficient information about residues governing the pH-effects on the catalytic activity leads to ambiguous assignments of the general acid and base catalysts and consequently its catalytic mechanism. In the present work, we use pH-replica exchange molecular dynamics (pH-REMD) simulations to study the effects of pH on E. coli GAR Tfase enzyme. We identify the titratable residues governing the pH-dependent conformational changes in the system. Furthermore, we filter out the protonation states which are essential in maintaining the structural integrity, keeping the ligands bound and assisting the catalysis. We reproduce the experimental pH-activity curve by computing the population of key protonation states. Moreover, we provide a detailed description of residues governing the acidic and basic limbs of the pH-activity curve.</div>

NEW TiO2-Ag NANOPARTICLES USED FOR ORGANIC COMPOUNDS DEGRADATION

2019 ◽  
Vol 18 (8) ◽  
pp. 1755-1763 ◽  
Author(s):  
Maria Harja ◽  
Igor Cretescu ◽  
Consuelo Gomez de Castro ◽  
Catalina Nutescu Duduman ◽  
Doina Lutic ◽  
...  
Keyword(s):  
Organic Compounds ◽  
Ag Nanoparticles
Sign in / Sign up

Export Citation Format

Share Document