Structure of Mixed Reverse Microemulsions Based on Sodium Bis (2‐Ethylhexyl) Sulfosuccinate and Sodium Cholate

2019 ◽  
Vol 23 (2) ◽  
pp. 339-346
Author(s):  
Irma Tikanadze ◽  
Manoni Kurtanidze ◽  
Marina Rukhadze ◽  
Ketevan Nanobashvili ◽  
Polina Toidze ◽  
...  
Keyword(s):  
Sodium Cholate ◽  
Reverse Microemulsions

Self-assembled luminescent cholate gels induced by a europium ion in deep eutectic solvents

Soft Matter ◽  
2021 ◽  
Author(s):  
Meng Sun ◽  
Qintang Li ◽  
Xiao Chen
Keyword(s):  
Self Assembly ◽  
Choline Chloride ◽  
Deep Eutectic Solvents ◽  
Sodium Cholate ◽  
The Self ◽  
Europium Ion ◽  
Self Assembled

Luminescent gels have been successfully fabricated through the self-assembly of sodium cholate and a europium ion in choline chloride-based deep eutectic solvents.

Sulfated Zirconia Nanoparticles Synthesized in Reverse Microemulsions:  Preparation and Catalytic Properties

Langmuir ◽  
2002 ◽  
Vol 18 (20) ◽  
pp. 7428-7435 ◽  
Author(s):  
Holger Althues ◽  
Stefan Kaskel
Keyword(s):  
Sulfated Zirconia ◽  
Catalytic Properties ◽  
Reverse Microemulsions ◽  
Zirconia Nanoparticles

The structure of sodium 3α,7α,12α-trihydroxy-5β-cholan-24-oate monohydrate (sodium cholate monohydrate)

1980 ◽  
Vol 36 (2) ◽  
pp. 287-292 ◽  
Author(s):  
R. E. Cobbledick ◽  
F. W. B. Einstein
Keyword(s):  
Sodium Cholate

Interactions in Aqueous Mixtures of Alkylammonium Chlorides and Sodium Cholate

2006 ◽  
Vol 27 (8) ◽  
pp. 1099-1111 ◽  
Author(s):  
M. Vinceković ◽  
D. Jurašin ◽  
V. Tomašić ◽  
M. Bujan ◽  
N. Filipović‐Vinceković
Keyword(s):  
Sodium Cholate ◽  
Aqueous Mixtures

Acetylsalicylic acid hydrolase of gastric mucosa.

1978 ◽  
Vol 234 (6) ◽  
pp. E606
Author(s):  
J G Spenney
Keyword(s):  
Gastric Mucosa ◽  
Enzymatic Activity ◽  
Acetylsalicylic Acid ◽  
Sodium Dodecyl ◽  
Sodium Cholate ◽  
Acid Hydrolase ◽  
Sulfhydryl Reagents ◽  
Ph Optimum ◽  
Diisopropyl Fluorophosphate

Acetylsalicylic acid hydrolase activity of rabbit fundic gastric mucosa has been isolated from the soluble 100,000 X g supernate. The enzymatic activity was partially purified by ammonium sulfate precipitation. The Km for acetylsalicylate was 2 mM and pH optimum was 8.6. The activity was insensitive to ionic strength, slightly inhibited by inclusion of 100 mM Cl-, and demonstrated no requirement for Ca2+ or Mg2+. Acetylsalicylic acid esterase was markedly inhibited by sodium cholate and sodium dodecyl sulfate. The enzyme was insensitive to sulfhydryl reagents with the exception of p-chloromercuribenzenesulfonic acid, which markedly inhibited the enzyme. Diisopropyl fluorophosphate (DFP) inhibited enzymatic activity with a Ki of 9 X 10(-9)M. Eserine was also inhibitory with a Ki of 0.25 mM. Inhibition by DFP at low concentration and by eserine at millimolar concentrations suggests that this enzyme is related to the group of aliphatic esterases. Identification of potent inhibitors will enable studies to define the role of this enzyme with the use of experimental preparations in which systemic toxicity can be avoided.

Excystment of the Metacercariae of Echinoparyphium serratum (Trematoda: Echinostomatidae)

1970 ◽  
Vol 44 (1) ◽  
pp. 35-56 ◽  
Author(s):  
M. J. Howell
Keyword(s):  
Elevated Temperature ◽  
Cyst Wall ◽  
Sodium Dithionite ◽  
Sodium Cholate ◽  
Stage I ◽  
Combined Effects ◽  
Active Process ◽  
Reducing Conditions ◽  
Exogenous Enzymes ◽  
Pretreatment Solution

1. Metacercarial cysts of Echinoparyphium serratum occur in the pericardium of the snail Isidorella brazieri. Each cyst is surrounded by a nucleated, syncytial host capsule containing granules which are presumed to be melanin. The cyst wall consists of two layers and both contain acid and neutral mucopolysaccharide but little or no protein. No modification of the cyst wall coincident with the point of emergence of the metacercaria has been located.2. Excystment of the metacercaria takes place in two main stages when pepsin is omitted from the initial pretreatment solution: stage I (emergence from the cyst wall through the escape aperture) is an active process (exogenous enzymes are not necessary), and a high percentage of specimens reaching this stage is dependent on the combined effects of a þH of 2, reducing conditions, elevated temperature (37–39°C) and sodium cholate. Temperature and sodium cholate are absolute requirements for this stage as is pretreatment of between þH 2 and 4 when sodium cholate is included with the reductant (sodium dithionite) rather than in the excystment medium with trypsin. The possibility that CO2 is involved has not been established.

scholarly journals Probing the Action of Permeation Enhancers Sodium Cholate and N-dodecyl-β-D-maltoside in a Porcine Jejunal Mucosal Explant System

Pharmaceutics ◽  
2018 ◽  
Vol 10 (4) ◽  
pp. 172 ◽  
Author(s):  
E. Danielsen ◽  
Gert Hansen
Keyword(s):  
Brush Border ◽  
Lucifer Yellow ◽  
Membrane Integrity ◽  
Sodium Cholate ◽  
Permeability Barrier ◽  
Permeation Enhancers ◽  
Uptake Mechanism ◽  
Cell Membrane Integrity ◽  
Apical Extrusion ◽  
Small Intestinal

The small intestinal epithelium constitutes a major permeability barrier for the oral administration of therapeutic drugs with poor bioavailability, and permeation enhancers (PEs) are required to increase the paracellular and/or transcellular uptake of such drugs. Many PEs act as surfactants by perturbing cell membrane integrity and causing permeabilization by leakage or endocytosis. The aim of the present work was to study the action of sodium cholate (NaC) and N-dodecyl-β-D-maltoside (DDM), using a small intestinal mucosal explant system. At 2 mM, both NaC and DDM caused leakage into the enterocyte cytosol of the fluorescent probe Lucifer Yellow, but they also blocked the constitutive endocytotic pathway from the brush border. In addition, an increased paracellular passage of 3-kDa Texas Red Dextran into the lamina propria was observed. By electron microscopy, both PEs disrupted the hexagonal organization of microvilli of the brush border and led to the apical extrusion of vesicle-like and amorphous cell debris to the lumen. In conclusion, NaC and DDM acted in a multimodal way to increase the permeability of the jejunal epithelium both by paracellular and transcellular mechanisms. However, endocytosis, commonly thought to be an uptake mechanism that may be stimulated by PEs, was not involved in the transcellular process.

Cholate inhibits high-fat diet-induced hyperglycemia and obesity with acyl-CoA synthetase mRNA decrease

1997 ◽  
Vol 273 (1) ◽  
pp. E37-E45 ◽  
Author(s):  
S. Ikemoto ◽  
M. Takahashi ◽  
N. Tsunoda ◽  
K. Maruyama ◽  
H. Itakura ◽  
...  
Keyword(s):  
High Fat Diet ◽  
Skeletal Muscles ◽  
Unsaturation Index ◽  
Sodium Cholate ◽  
Fat Absorption ◽  
High Fat ◽  
Cholesterol Accumulation ◽  
Triglyceride Accumulation ◽  
Responsive Element

The effects of sodium cholate on high-fat diet-induced hyperglycemia and obesity were investigated. Insulin resistance was estimated by measuring 2-deoxyglucose uptake in epitrochlearis muscles incubated in vitro. Addition of 0.5% cholate to high-safflower oil diet completely prevented high fat-induced hyperglycemia and obesity in C57BL/6J mice with a slight decrease of energy intake but with no inhibition of fat absorption. Furthermore, the addition of cholate decreased blood insulin levels and prevented high-fat diet-induced decrease of glucose uptake in epitrochlearis. However, there was no change in the unsaturation index of fatty acids in skeletal muscles and in GLUT-4 levels by cholate. In liver, cholate addition resulted in cholesterol accumulation and completely prevented high-fat diet-induced triglyceride accumulation. The changes of triglyceride level in the liver were paralleled to the changes of acyl-CoA synthetase (ACS) mRNA. ACS catalyzes the formation of acyl-CoA from fatty acid, and acyl-CoA is utilized for triglyceride formation in liver. ACS has a sterol-responsive element 1 in its promoter region. These data indicate that the favorable effects of cholate could be partly the result of downregulation of ACS mRNA.

scholarly journals The glycosylation properties of D2 dopamine receptors from striatal and limbic areas of bovine brain

1988 ◽  
Vol 255 (3) ◽  
pp. 877-883 ◽  
Author(s):  
M N Leonard ◽  
R A Williamson ◽  
P G Strange
Keyword(s):  
Caudate Nucleus ◽  
Dopamine Receptors ◽  
Sodium Cholate ◽  
Bovine Brain ◽  
Affinity Column ◽  
Olfactory Tubercle ◽  
D2 Dopamine Receptors ◽  
Neuraminidase Treatment ◽  
Membrane Bound ◽  
Affinity Interaction

D2 dopamine receptors from bovine brain (caudate nucleus and olfactory tubercle) have been solubilized using sodium cholate/NaCl and their glycoprotein properties studied in terms of their interaction with wheat-germ agglutinin-agarose (WGA-agarose). Under optimal conditions about 65% of the applied D2 dopamine receptors bound to WGA-agarose and could be eluted with N-acetylglucosamine. The ability of receptors to adsorb to the affinity column was shown to be dependent on the cholate and salt concentrations used. Digestion of the membrane bound D2 dopamine receptors with neuraminidase prior to solubilisation reduced the ability of the receptors to bind to WGA-agarose (50% of applied receptors bound) whereas digestion with N-acetylglucosaminidase did not significantly affect binding to WGA-agarose. Digestion with the two enzymes together resulted in a larger decrease in binding to WGA-agarose than was seen with the two enzymes alone (40% of applied receptors bound). Stepwise elution of bound receptors from the WGA-agarose columns using 2.5 mM- and 100-mM-N-acetylglucosamine showed that about 40% of the bound receptors interacted with WGA-agarose in a low-affinity manner, the remainder showing a high-affinity interaction. Neuraminidase treatment reduced the low-affinity population suggesting that the interaction of oligosaccharides bearing sialic acid with WGA-agarose is of lower affinity and that higher-affinity binding is via N-acetylglucosamine. These data are discussed in terms of the heterogeneity of carbohydrate moieties on the D2 dopamine receptors within a brain region. In all the tests applied here, however, receptors from caudate nucleus and olfactory tubercle behaved identically so their glycosylation patterns must be very similar.

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