Selective recognition of fluoride anion in water by a copper(ii) center embedded in a hydrophobic cavity

2014 ◽  
Vol 5 (10) ◽  
pp. 3897-3904 ◽  
Author(s):  
Andrea Brugnara ◽  
Filip Topić ◽  
Kari Rissanen ◽  
Aurélien de la Lande ◽  
Benoit Colasson ◽  
...  
Keyword(s):  
Selective Recognition ◽  
Fluoride Anion ◽  
Hydrophobic Pocket ◽  
Hydrophobic Cavity ◽  
Neutral Ph

CuII coordination combined with hydrophobic pocket hosting allows for strong and selective fluoride binding in water at near neutral pH.

Highly selective fluorescence sensors for the fluoride anion based on carboxylate-bridged diiron complexes

2016 ◽  
Vol 45 (16) ◽  
pp. 6839-6846 ◽  
Author(s):  
Yuhan Zhou ◽  
Xiaoliang Dong ◽  
Yixin Zhang ◽  
Peng Tong ◽  
Jingping Qu
Keyword(s):  
Selective Recognition ◽  
Fluoride Anion ◽  
Fluoride Ion ◽  
Fluorescence Sensors

The diiron–sulfur clusters bearing urea and anthracene units showed rapid and selective recognition for the fluoride ion.

scholarly journals A simple naphthalimide-based receptor for selective recognition of fluoride anion

ARKIVOC ◽  
2012 ◽  
Vol 2013 (2) ◽  
pp. 133-145
Author(s):  
Arvind Misra ◽  
Mohammad Shahid ◽  
Pratibha Dwivedi ◽  
Priyanka Srivastava ◽  
Rashid Ali ◽  
...  
Keyword(s):  
Selective Recognition ◽  
Fluoride Anion

Naked eye detection of anions by alkynyl-ruthenium exo-receptors: selective recognition of fluoride anion

2005 ◽  
pp. 2924 ◽  
Author(s):  
Jean-Luc Fillaut ◽  
Julien Andriès ◽  
Loïc Toupet ◽  
Jean-Pierre Desvergne
Keyword(s):  
Selective Recognition ◽  
Fluoride Anion ◽  
Eye Detection ◽  
Naked Eye ◽  
Naked Eye Detection

Selective Recognition of Fluoride Anion Using a Li+-Metallacrown Complex

2002 ◽  
Vol 41 (8) ◽  
pp. 1419-1422 ◽  
Author(s):  
Marie-Line Lehaire ◽  
Rosario Scopelliti ◽  
Holger Piotrowski ◽  
Kay Severin
Keyword(s):  
Selective Recognition ◽  
Fluoride Anion

Selective Recognition of Fluoride Anion Using a Li+–Metallacrown Complex

2002 ◽  
Vol 114 (8) ◽  
pp. 1477 ◽  
Author(s):  
Marie-Line Lehaire ◽  
Rosario Scopelliti ◽  
Holger Piotrowski ◽  
Kay Severin
Keyword(s):  
Selective Recognition ◽  
Fluoride Anion

Examination of Rabbit Fc Crystals

1968 ◽  
Vol 26 ◽  
pp. 140-141
Author(s):  
J. P. Robinson ◽  
P. G. Lenhert
Keyword(s):  
Molecular Weight ◽  
Flat Plate ◽  
Phosphate Buffer ◽  
Asymmetric Unit ◽  
X Ray Diffraction ◽  
X Ray ◽  
Neutral Ph ◽  
Small Crystals ◽  
Carbon Coated ◽  
Diffraction Patterns

Crystallographic studies of rabbit Fc using X-ray diffraction patterns were recently reported. The unit cell constants were reported to be a = 69. 2 A°, b = 73. 1 A°, c = 60. 6 A°, B = 104° 30', space group P21, monoclinic, volume of asymmetric unit V = 148, 000 A°3. The molecular weight of the fragment was determined to be 55, 000 ± 2000 which is in agreement with earlier determinations by other methods.Fc crystals were formed in water or dilute phosphate buffer at neutral pH. The resulting crystal was a flat plate as previously described. Preparations of small crystals were negatively stained by mixing the suspension with equal volumes of 2% silicotungstate at neutral pH. A drop of the mixture was placed on a carbon coated grid and allowed to stand for a few minutes. The excess liquid was removed and the grid was immediately put in the microscope.

CHEMICAL EFFECTS IN MULTIELECTRON PROCESSES IN THE FLUORIDE ANION

1987 ◽  
Vol 48 (C9) ◽  
pp. C9-777-C9-780
Author(s):  
R. HESSABI ◽  
D. URCH
Keyword(s):  
Fluoride Anion ◽  
Chemical Effects

Reaction of Acetaldehyde with Human Platelets

1992 ◽  
Vol 67 (01) ◽  
pp. 126-130 ◽  
Author(s):  
Olivier Spertini ◽  
Jacques Hauert ◽  
Fedor Bachmann
Keyword(s):  
Platelet Aggregation ◽  
Inhibitory Action ◽  
Ex Vivo ◽  
Platelet Rich Plasma ◽  
Shape Change ◽  
Reaction Medium ◽  
Human Platelets ◽  
Membrane Glycoproteins ◽  
Neutral Ph

SummaryPlatelet function defects observed in chronic alcoholics are not wholly explained by the inhibitory action of ethanol on platelet aggregation; they are not completely reproduced either in vivo by short-term ethanol perfusion into volunteers or in vitro by the addition of ethanol to platelet-rich plasma. As acetaldehyde (AcH) binds to many proteins and impairs cellular activities, we investigated the effect of this early degradation product of ethanol on platelets. AcH formed adducts with human platelets at neutral pH at 37° C which were stable to extensive washing, trichloracetic acid hydrolysis and heating at 100° C, and were not reduced by sodium borohydride. The amount of platelet adducts formed was a function of the incubation time and of the concentration of AcH in the reaction medium. At low AcH concentrations (<0.2 mM), platelet bound AcH was directly proportional to the concentration of AcH in the reaction medium. At higher concentrations (≥0.2 mM), AcH uptake by platelets tended to reach a plateau. The amount of adducts was also proportional to the number of exposures of platelets to pulses of 20 pM AcH.AcH adducts formation severely impaired platelet aggregation and shape change induced by ADP, collagen and thrombin. A positive correlation was established between platelet-bound AcH and inhibition of aggregation.SDS-PAGE analysis of AcH adducts at neutral pH demonstrated the binding of [14C]acetaldehyde to many platelet proteins. AcH adduct formation with membrane glycoproteins, cytoskeleton and enzymes might interfere with several steps of platelet activation and impair platelet aggregation.This in vitro study shows that AcH has a major inhibitory action on platelet aggregation and may account for the prolonged ex vivo inhibition of aggregation observed in chronic alcoholics even in the absence of alcoholemia.

Preparation, Stabilization and Some Properties of Purified Human Plasmin*

1964 ◽  
Vol 11 (01) ◽  
pp. 075-084 ◽  
Author(s):  
Daniel L Kline ◽  
Jacob B Fishman ◽  
Keyword(s):  
Plasminogen Activator ◽  
Stable Form ◽  
Neutral Ph ◽  
The Stability ◽  
And Storage

Summary1. Lysine increased the solubility, decreased the SK requirement and increased the stability of plasmin prepared from purified plasminogen by SK activation.2. A procedure is presented for the rapid and quantitative conversion of plasminogen to plasmin and storage of the plasmin in stable form at neutral pH as a lyophilized powder.3. Approximately 10% for the plasminogen molecule was split off during its activation. No carbohydrate was lost.4. The plasmin isolated was homogeneous in the ultracentrifuge at pH 2.5 and was quantitatively convertible to plasminogen activator by the addition of SK.

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