Solid–Liquid Equilibria of KCl in Polyethylene Glycol 6000–H2O Mixed Solvent at 288.2, 298.2, and 308.2 K: Experiment and Correlation

2020 ◽  
Vol 53 (6) ◽  
pp. 229-236
Author(s):  
Xudong Yu ◽  
Qin Huang ◽  
Miangping Zheng ◽  
Lin Wang ◽  
Maolan Li
Keyword(s):  
Polyethylene Glycol ◽  
Mixed Solvent ◽  
Solid Liquid ◽  
Polyethylene Glycol 6000

Hepatitis a Virus Concentration from Experimentally Contaminated Distilled, Tap, Waste and Seawater

1989 ◽  
Vol 21 (3) ◽  
pp. 255-258 ◽  
Author(s):  
Evangélos Biziagos ◽  
Jacques Passagot ◽  
Jean-Marc Crance ◽  
Robert Deloince
Keyword(s):  
Cell Culture ◽  
Polyethylene Glycol ◽  
Hepatitis A ◽  
Hepatitis A Virus ◽  
Tap Water ◽  
Virus Concentration ◽  
Beef Extract ◽  
Polyethylene Glycol 6000

The concentration of cell-culture-adapted hepatitis A virus (HAV) from experimentally contaminated distilled, drinking, waste and seawater was performed by using a filter adsorption-elu-tion method in the following conditions: HAV seeded in water was adsorbed at pH 4.0 to two nitrocellulose membranes (1.2 and 0.45 µm porosity for distilled and tap water or 8.0 and 3.0 µm porosity for waste and seawater), then eluted by 3% beef-extract at pH 8.5 and further concentrated by polyethylene glycol 6000 precipitation. Thus, HAV in 5 to 50 liters of seeded waters was concentrated approximately 1,700 to 17,000 fold with greater than 70% recovery of the initial virus added to the samples.

A new automated turbidimetric immunoassay for quantifying alpha 1-antitrypsin in serum.

1986 ◽  
Vol 32 (6) ◽  
pp. 1020-1022 ◽  
Author(s):  
J A Viedma ◽  
A de la Iglesia ◽  
M Parera ◽  
M T López
Keyword(s):  
Polyethylene Glycol ◽  
Parametric Estimation ◽  
Tween 20 ◽  
Upper Limit ◽  
Analytical Recovery ◽  
The Mean ◽  
Alpha 1 Antitrypsin ◽  
Polyethylene Glycol 6000 ◽  
Immunoprecipitation Reaction ◽  
Turbidimetric Immunoassay

Abstract This rapid, sensitive equilibrium turbidimetric immunoassay for quantification of alpha 1-antitrypsin involves a monospecific antibody, polyethylene glycol 6000 to accelerate and enhance the immunoprecipitation reaction, and Tween 20 surfactant to decrease and stabilize the sample-blank values. Turbidity at 334 nm is measured by an automated discrete analyzer. Grossly lipemic, icteric, or hemolyzed samples can be assayed. Correlation with results by radial immunodiffusion (RID) was excellent (r = 0.97, n = 84). Analytical recovery averaged 97.7 (SD 2.9)%. Within-run CVs ranged from 1.6 to 1.9%, between-day CVs from 2.0 to 3.5%. Reference values for healthy adults (n = 147) were determined by parametric estimation (for an assumed normal distribution of untransformed data). The lower limit (g/L) with its 0.90 confidence interval is 1.23 (range 1.18-1.28), the upper limit is 2.15 (2.10-2.20), and the mean is 1.69 g/L.

N-Ethylmaleimide-modified actin filaments do not bundle in the presence of α-actinin

1995 ◽  
Vol 73 (1-2) ◽  
pp. 116-122 ◽  
Author(s):  
Aldo Milzani ◽  
Isabella DalleDonne ◽  
Roberto Colombo
Keyword(s):  
Polyethylene Glycol ◽  
Chemical Modification ◽  
Molecular Interactions ◽  
Binding Sites ◽  
Actin Filaments ◽  
Actin Assembly ◽  
Chemically Modified ◽  
C Terminus ◽  
Spatial Reorganization ◽  
Polyethylene Glycol 6000

We show that the modification of actin subdomain 1 by N-ethylmaleimide (NEM), which binds Cys-374 close to the C-terminus of the molecule, inhibits the α-actinin-induced bundling of actin filaments. This effect is not merely related to the block of Cys-374, since N-(1-pyrenyl)iodoacetamide (pyrene-IA) is unable to prevent bundling. Considering that NEM (but not pyrene-IA) influences actin assembly, we suggest that the inhibition of the actin – α-actinin interaction is due to the chemical modification of actin Cys-374 which, by inducing a marked spatial reorganization of actin monomers, is able to modify both the intra- and inter-molecular interactions of this protein. Finally, NEM-modified actin filaments form bundles in the presence of polyethylene glycol 6000 since, in this case, the side by side association of actin filaments does not depend on the accessibility of binding sites nor on the formation of chemical bonds.Key words: chemically modified actin, N-ethylmaleimide, pyrene-IA, Cys-374, actin bundles, α-actinin.

scholarly journals Rapid Assay of Trace Immunoglobulin M by a New Immunonanogold Resonance Scattering Spectral Probe

2008 ◽  
Vol 13 (4) ◽  
pp. 302-308 ◽  
Author(s):  
Zhiliang Jiang ◽  
Lili Wei ◽  
Mingjing Zou ◽  
Aihui Liang ◽  
Mianwu Meng
Keyword(s):  
Polyethylene Glycol ◽  
Detection Limit ◽  
Resonance Scattering ◽  
Immunoglobulin M ◽  
Serum Samples ◽  
Rapid Assay ◽  
Lower Detection Limit ◽  
Lower Detection ◽  
Polyethylene Glycol 6000

Nanogold, 8 nm in size, was used to label goat antihuman immunoglobulin M (GIgM) to obtain a new immunonanogold resonance scattering (RS) probe (Au-GIgG) for quantitation of trace immunoglobulin M (IgM). The Au-GIgG combined with IgM to form nanogold-labeled immunocomplex causes the RS intensity at 580 nm to be enhanced, in pH 4.49 KH2PO 4-Na2HPO4 buffer and in the presence of polyethylene glycol 6000. The enhanced RS intensity at 580 nm (ΔI580 nm) is proportional to the IgM concentration in the range of 1.5 to 2000 ng/mL, with a lower detection limit of 0.98 ng/mL. The immunonanogold RS assay was used to assay IgM in serum samples, with sensitivity, selectivity, and simplicity. ( Journal of Biomolecular Screening 2008:302-308)

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