A thermodynamic model for silica and aluminum in alkaline solutions with high ionic strength at elevated temperatures up to 100  C: Applications to zeolites

2012 ◽  
Vol 98 (1) ◽  
pp. 141-153 ◽  
Author(s):  
Y. Xiong
Keyword(s):  
Ionic Strength ◽  
Thermodynamic Model ◽  
Elevated Temperatures ◽  
High Ionic Strength ◽  
Alkaline Solutions

scholarly journals The mitochondrial localization of coproporphyrinogen III oxidase

1978 ◽  
Vol 176 (1) ◽  
pp. 97-102 ◽  
Author(s):  
B Grandchamp ◽  
N Phung ◽  
Y Nordmann
Keyword(s):  
Ionic Strength ◽  
Rat Liver ◽  
Membrane Binding ◽  
High Ionic Strength ◽  
Alkaline Solutions ◽  
Intermembrane Space ◽  
Mitochondrial Localization ◽  
Inner Membrane ◽  
Membrane Matrix ◽  
Coproporphyrinogen Iii Oxidase

The location of coproporphyrinogen III oxidase in mitochondria was studied in rat liver by using the digitonin method or hypo-osmotic media for fractionation. The enzyme was found in the intermembrane space with a fraction loosely bound to the inner membrane. This fraction was released by washing the inner-membrane-matrix complex with alkaline solutions or solutions of high ionic strength. The enzyme in both fractions had the same Km (0.16 micrometer) for coproporphyrinogen III. When incubation was performed in a medium that avoided destruction of enzyme membrane binding, a dramatic increase in activity was observed after sonication of whole mitochondria or of the inner-membrane-matrix complex.

Kinetics of Cyanate Decomposition in Alkaline Solutions of High Ionic Strength:  The Catalytic Effect of Bicarbonate

2004 ◽  
Vol 43 (16) ◽  
pp. 4815-4821 ◽  
Author(s):  
Nikolai DeMartini ◽  
Dmitry Yu. Murzin ◽  
Mikael Forssén ◽  
Mikko Hupa
Keyword(s):  
Ionic Strength ◽  
Catalytic Effect ◽  
High Ionic Strength ◽  
Alkaline Solutions ◽  
Kinetics Of

Neptunium(VII) in high-ionic-strength alkaline solutions — [NpO2(OH)4]1– or [NpO4(OH)2]3–?

2009 ◽  
Vol 87 (10) ◽  
pp. 1436-1443 ◽  
Author(s):  
John E. C. Wren ◽  
Georg Schreckenbach
Keyword(s):  
Ionic Strength ◽  
Density Functional ◽  
Chemical Shifts ◽  
Structural Data ◽  
High Ionic Strength ◽  
Alkaline Solutions ◽  
Recent Experimental Data ◽  
Central Metal ◽  
Functional Theory ◽  
Coordination Environment

Relativistic density functional theory (ZORA-PBE, COSMO solvation) is used to address the title question, based on comparison with recent experimental data ( 1 ). Structural data (bond lengths), vibrational frequencies, and 17O NMR chemical shifts are used to prove that [NpO4(OH)2]3– is the predominant species in high-ionic-strength alkaline solutions of NpVII. Neptunium(VII) complexes have stronger bonds than their formally isoelectronic uranium(VI) analogues. The experimentally observed 300 ppm shift in 17O chemical shifts between the known [UO2(OH)4]2– and NpVII solution is shown to be partly a function of the central metal (NpVII vs. UVI) and not of the coordination environment (tetraoxo vs. dioxo). Comparing, for a given An (UVI or NpVII), actinyl complexes [AnO2X4]2–/1–, X = Cl, F, OH, a decreasing strength of the axial actinyl bond is observed that is traced to electronic factors (equatorial π-competition).

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

1976 ◽  
Vol 35 (01) ◽  
pp. 186-190 ◽  
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.

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

1978 ◽  
Vol 88 (2) ◽  
pp. 298-305 ◽  
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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