Sodium carboxymethyl cellulose modulates the stability of cinnamaldehyde-loaded liposomes at high ionic strength

In this paper, the effect of sodium lignosulfonate and sodium carboxymethyl cellulose on the stability of a water-coal suspension was studied. As a result, the viscosity of the water-coal suspension was 0.01-0.08 P∙s. The change in dynamic shear rate was considered when adding these plasticizers in different changes. The minimum value of the dynamic shear rate of 13.6 was achieved with the addition of sodium LST plasticizer (SD = 0.1%) in the presence of 40% coal. The influence of alkali on the viscosity of a water-coal suspension was also studied.

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Complexation of americium with humic, fulvic and citric acids at high ionic strength

Radiochimica Acta ◽

10.1524/ract.2002.90.9-11_2002.563 ◽

2002 ◽

Vol 90 (9-11) ◽

Cited By ~ 21

Author(s):

N. A. Wall ◽

M. Borkowski ◽

J. Chen ◽

Gregory R. Choppin

Keyword(s):

Ionic Strength ◽

Stability Constants ◽

High Ionic Strength ◽

The Stability

SummaryThe stability constants of the Am

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Study of the Stability of Functionalized Gold Nanoparticles for the Colorimetric Detection of Dipeptidyl Peptidase IV

Applied Sciences ◽

10.3390/app8122589 ◽

2018 ◽

Vol 8 (12) ◽

pp. 2589 ◽

Cited By ~ 8

Author(s):

Hasan Aldewachi ◽

Nicola Woodroofe ◽

Philip Gardiner

Keyword(s):

Gold Nanoparticles ◽

Ionic Strength ◽

Biomedical Applications ◽

Colorimetric Detection ◽

Dipeptidyl Peptidase ◽

High Ionic Strength ◽

Dipeptidyl Peptidase Iv ◽

Au Nps ◽

Dpp Iv ◽

The Stability

In this report, we investigated three stabilization strategies of gold nanoparticles and their practical application for the visual detection of dipeptidyl peptidase IV (DPP-IV). Citrate-capped gold nanoparticles (Au NPs) are generally unstable in high-ionic-strength samples. Au NPs are easily tagged with various proteins and biomolecules rich in amino acids, leading to important biomedical applications including targeted drug delivery, cellular imaging, and biosensing. The investigated assays were based on different modes of stabilization, such as the incorporation of polyethylene glycol (PEG) groups, stabilizer peptide, and bifunctionalization. Although all approaches provided highly stable Au NP platforms demonstrated by zeta potential measurements and resistance to aggregation in a high-ionic-strength saline solution, we found that the Au NPs modified with a separate stabilizer ligand provided the highest stability and was the only platform that demonstrated sensitivity to the addition of DPP-IV, whilst PEGylated and peptide-stabilized Au NPs showed no significant response.

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Importance of Protease Inhibition in Studies on Purified Factor VIII (Antihaemophilic Factor)

Thrombosis and Haemostasis ◽

10.1055/s-0038-1647943 ◽

1976 ◽

Vol 35 (01) ◽

pp. 186-190 ◽

Cited By ~ 6

Author(s):

Eugen A. Beck ◽

Peter Bachmann ◽

Peter Barbier ◽

Miha Furlan

Keyword(s):

Ionic Strength ◽

Factor Viii ◽

Gel Filtration ◽

High Ionic Strength ◽

Procoagulant Activity ◽

Carrier Protein ◽

Protease Inhibition ◽

Functional Sites ◽

Molecular Weight Peak ◽

Von Willebrand

SummaryAccording to some authors factor VIII procoagulant activity may be dissociable from carrier protein (MW~ 2 × 106) by agarose gel filtration, e.g. at high ionic strength. We were able to reproduce this phenomenon. However, addition of protease inhibitor (Trasylol) prevented the appearance of low molecular weight peak of factor VIII procoagulant activity both at high ionic strength and elevated temperature (37°C). We conclude from our results that procoagulant activity and carrier protein (von Willebrand factor, factor VIII antigen) are closely associated functional sites of native factor VIII macro molecule. Consequently, proteolytic degradation should be avoided in functional and structural studies on factor VIII and especially in preparing factor VIII concentrate for therapeutic use.

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THE RELATIVE DISTRIBUTION OF THYROXINE, TRIIODOTHYRONINE AND 3,3′,5′-(REVERSE)-TRIIODOTHYRONINE IN VARIOUS FRACTIONS OF THYROGLOBULIN

Acta Endocrinologica ◽

10.1530/acta.0.0880298 ◽

1978 ◽

Vol 88 (2) ◽

pp. 298-305 ◽

Cited By ~ 2

Author(s):

Peter Laurberg

Keyword(s):

Ionic Strength ◽

Guinea Pig ◽

Sucrose Gradient ◽

Deae Cellulose ◽

High Ionic Strength ◽

Relative Distribution ◽

Thyroid Extract ◽

Reverse Triiodothyronine ◽

Thyroid Secretion ◽

Stable Iodine

ABSTRACT Thyroglobulin fractions rich and poor in new thyroglobulin were separated by means of DEAE-cellulose chromatography of dog thyroid extracts and by zonal ultracentrifugation in a sucrose gradient of guinea pig thyroid extract incubated at low temperature. The distribution of thyroxine, triiodothyronine and 3,3′,5′-(reverse)-triiodothyronine in hydrolysates of the different fractions was estimated by radioimmunoassays. Following DEAE-cellulose chromatography there was a small but statistically significant increase in the T4/T3 ratio in thyroglobulin fractions eluted at high ionic strength - that is fractions relatively rich in stable iodine but poor in fresh thyroglobulin. There were no differences in the T4/rT3 ratios between the different fractions. The ratios between iodothyronines were almost identical in the various thyroglobulin fractions following zonal ultracentrifugation in a sucrose gradient of cold treated guinea pig thyroid extract. These findings lend no support to the possibility that a relatively high content of triiodothyronines in freshly synthesized thyroglobulin modulates the thyroid secretion towards a preferential secretion of triiodothyronine and 3,3′,5′-(reverse)-triiodothyronine at the expense of the secretion of thyroxine.

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