The activity and stability of alkaline phosphatase in solutions of water and the fused salt ethylammonium nitrate

1984 ◽  
Vol 13 (8) ◽  
pp. 583-587 ◽  
Author(s):  
David K. Magnuson ◽  
James W. Bodley ◽  
D. Fennell Evans
Keyword(s):  
Alkaline Phosphatase ◽  
Ethylammonium Nitrate ◽  
Fused Salt

Micelle formation in ethylammonium nitrate, a low-melting fused salt

1982 ◽  
Vol 88 (1) ◽  
pp. 89-96 ◽  
Author(s):  
D.Fennell Evans ◽  
Akira Yamauchi ◽  
Ronald Roman ◽  
Ethel Z Casassa
Keyword(s):  
Micelle Formation ◽  
Ethylammonium Nitrate ◽  
Fused Salt

Diels-Alder reactions in ethylammonium nitrate, a low-melting fused salt

1989 ◽  
Vol 30 (14) ◽  
pp. 1785-1788 ◽  
Author(s):  
David A. Jaeger ◽  
Charles E. Tucker
Keyword(s):  
Diels Alder ◽  
Ethylammonium Nitrate ◽  
Fused Salt

Propriétés volumiques du nitrate d'éthylammonium fondu à 298 K et de ses mélanges avec l'eau

1985 ◽  
Vol 63 (3) ◽  
pp. 565-570 ◽  
Author(s):  
M. Hadded ◽  
M. Biquard ◽  
P. Letellier ◽  
R. Schaal
Keyword(s):  
Molar Volume ◽  
Salt Water ◽  
Pure Water ◽  
Molar Fraction ◽  
Partial Molar Volumes ◽  
Intrinsic Volume ◽  
Ethylammonium Nitrate ◽  
Actual Volume ◽  
Concentrated Solution ◽  
Fused Salt

Partial molar volumes of water and ethylammonium nitrate EAN are determined accurately in all water–EAN mixtures, between pure water and pure fused salt at 298 K. It has been found that the partial molar volume of water decreases linearly with molar fraction of salt, x, in concentrated solution of EAN (C > 2 mol L−1, x > 0.04). The main thermodynamic relations are established to describe the volumetric behaviour of salt, water, and solution. It has been shown that the intrinsic volume of salt can be identified roughly with the molar volume of the pure fused salt and the value of apparent molar volume of water with the actual volume of water in solution.

Pressions de vapeur des mélanges eau – nitrate d'éthylammonium à 298,15 K. Propriétés thermodynamiques des milieux eau – sel fondu

1985 ◽  
Vol 63 (12) ◽  
pp. 3587-3592 ◽  
Author(s):  
M. Biquard ◽  
P. Letellier ◽  
M. Fromon
Keyword(s):  
Activity Coefficient ◽  
Empirical Equation ◽  
Pure Water ◽  
Partial Molar Volumes ◽  
Pressure Measurements ◽  
Text Interpretation ◽  
Wide Range ◽  
Ethylammonium Nitrate ◽  
Vapor Pressure Measurements ◽  
Fused Salt

The activity and activity coefficient of water in water and ethylammonium nitrate (EAN) mixtures were determined by vapor pressure measurements between pure water and pure fused salt at 298.15 K. For a wide range of mole fractions of salt, (0.3 < X ≤ 1) the behaviour of water can be described very accurately by a "one parameter" empirical equation which involves activity coefficient, γE, mole fraction of EAN, and limiting Gibbs energy of the dilution of water in pure fused salt, [Formula: see text]:[Formula: see text]Interpretation of experimental results was also attempted by use of the B.E.T. equation. It appears that the energy, ΔEd = E − EL, in those solutions is very low. Partial molar volumes of water and salt are also discussed in relation to empirical and B.E.T. equations. It can be shown that the two equations lead to similar results.

Interrelationship of the cellular distribution and secretion of regular structure (RS) protein in Bacillus licheniformis nm 105

1992 ◽  
Vol 50 (1) ◽  
pp. 712-713
Author(s):  
Xiaorong Zhu ◽  
Richard McVeigh ◽  
Bijan K. Ghosh
Keyword(s):  
Alkaline Phosphatase ◽  
Bacillus Licheniformis ◽  
Self Assembly ◽  
Gel Electrophoresis ◽  
Culture Supernatant ◽  
Regular Structure ◽  
The Self ◽  
Cellular Distribution ◽  
Structural Protein ◽  
Laboratory Cultures

A mutant of Bacillus licheniformis 749/C, NM 105 exhibits some notable properties, e.g., arrest of alkaline phosphatase secretion and overexpression and hypersecretion of RS protein. Although RS is known to be widely distributed in many microbes, it is rarely found, with a few exceptions, in laboratory cultures of microorganisms. RS protein is a structural protein and has the unusual properties to form aggregate. This characteristic may have been responsible for the self assembly of RS into regular tetragonal structures. Another uncommon characteristic of RS is that enhanced synthesis and secretion which occurs when the cells cease to grow. Assembled RS protein with a tetragonal structure is not seen inside cells at any stage of cell growth including cells in the stationary phase of growth. Gel electrophoresis of the culture supernatant shows a very large amount of RS protein in the stationary culture of the B. licheniformis. It seems, Therefore, that the RS protein is cotranslationally secreted and self assembled on the envelope surface.

In Situ Localization of PPAR Gamma and Uncoupling Protein in Mouse Embryo Sections Using Digoxigenin-Labeled Riboprobes

1996 ◽  
Vol 54 ◽  
pp. 32-33
Author(s):  
C. Jennermann ◽  
S. A. Kliewer ◽  
D. C. Morris
Keyword(s):  
Alkaline Phosphatase ◽  
Room Temperature ◽  
Uncoupling Protein ◽  
Ppar Gamma ◽  
Nuclear Hormone Receptor ◽  
Full Length ◽  
Northern Analysis ◽  
Peroxisome Proliferator

Peroxisome proliferator-activated receptor gamma (PPARg) is a member of the nuclear hormone receptor superfamily and has been shown in vitro to regulate genes involved in lipid metabolism and adipocyte differentiation. By Northern analysis, we and other researchers have shown that expression of this receptor predominates in adipose tissue in adult mice, and appears first in whole-embryo mRNA at 13.5 days postconception. In situ hybridization was used to find out in which developing tissues PPARg is specifically expressed.Digoxigenin-labeled riboprobes were generated using the Genius™ 4 RNA Labeling Kit from Boehringer Mannheim. Full length PPAR gamma, obtained by PCR from mouse liver cDNA, was inserted into pBluescript SK and used as template for the transcription reaction. Probes of average size 200 base pairs were made by partial alkaline hydrolysis of the full length transcripts. The in situ hybridization assays were performed as described previously with some modifications. Frozen sections (10 μm thick) of day 18 mouse embryos were cut, fixed with 4% paraformaldehyde and acetylated with 0.25% acetic anhydride in 1.0M triethanolamine buffer. The sections were incubated for 2 hours at room temperature in pre-hybridization buffer, and were then hybridized with a probe concentration of 200μg per ml at 70° C, overnight in a humidified chamber. Following stringent washes in SSC buffers, the immunological detection steps were performed at room temperature. The alkaline phosphatase labeled, anti-digoxigenin antibody and detection buffers were purchased from Boehringer Mannheim. The sections were treated with a blocking buffer for one hour and incubated with antibody solution at a 1:5000 dilution for 2 hours, both at room temperature. Colored precipitate was formed by exposure to the alkaline phosphatase substrate nitrobluetetrazoliumchloride/ bromo-chloroindlylphosphate.

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