Determination of dissociation constant of some quinazoline derivatives at different temperatures in DMF–water medium

2015 ◽  
Vol 201 ◽  
pp. 90-95 ◽  
Author(s):  
Shipra Baluja ◽  
Kajal Nandha
2020 ◽  
Vol 13 (1) ◽  
pp. 25-29
Author(s):  
Tanaji N. Bansode

Potentiometric titrations of phenothiazines derivatives were performed in methanolwater, ethanol-water, acetonitrile-water and dioxane-water mixtures with varying contents of organic solvent. All titrations were performed in aqua-organic medium at constant ionic strength (0.15 mol⋅dm−3) and at different temperatures (25 to 45 °C). The pKa were determined at different aqua-organic proportions. Effect of temperature and dielectric constant on dissociation constant has been compared. The pKa values were then obtained by Yasuda‐Shedlovsky extrapolation.


1985 ◽  
Vol 54 (02) ◽  
pp. 533-538 ◽  
Author(s):  
Wilfried Thiel ◽  
Ulrich Delvos ◽  
Gert Müller-Berghaus

SummaryA quantitative determination of soluble fibrin in plasma was carried out by affinity chromatography. For this purpose, desAA-fibrin and fibrinogen immobilized on Sepharose 4B were used at the stationary side whereas batroxobin-induced 125I-desAA-fibrin or thrombin-induced 125I-desAABB-fibrin mixed with plasma containing 131I-fibrinogen represented the fluid phase. The binding characteristics of these mixtures to the immobilized proteins were compared at 20° C and 37° C. Complete binding of both types of fibrin to the immobilized desAA-fibrin was always seen at 20° C as well as at 37° C. However, binding of soluble fibrin was accompanied by substantial binding of fibrinogen that was more pronounced at 20° C. Striking differences depending on the temperature at which the affinity chromatography was carried out, were documented for the fibrinogen-fibrin interaction. At 20° C more than 90% of the applied desAA-fibrin was bound to the immobilized fibrinogen whereas at 37° C only a mean of 17% were retained at the fibrinogen-Sepharose column. An opposite finding with regard to the tested temperature was made with the desAABB-fibrin. Nearly complete binding to insolubilized fibrinogen was found at 37° C (95%) but only 58% of the desAABB-fibrin were bound at 20° C. The binding patterns did not change when the experiments were performed in the presence of calcium ions. The opposite behaviour of the two types of soluble fibrin to immobilized fibrinogen at the different temperatures, together with the substantial binding of fibrinogen in the presence of soluble fibrin to insolubilized fibrin in every setting tested, devaluates affinity chromatography as a tool in the quantitative assessment of soluble fibrin in patients’ plasma.


Materials ◽  
2021 ◽  
Vol 14 (11) ◽  
pp. 3013
Author(s):  
Leszek Czechowski

The paper deals with an examination of the behaviour of glued Ti-Al column under compression at elevated temperature. The tests of compressed columns with initial load were performed at different temperatures to obtain their characteristics and the load-carrying capacity. The deformations of columns during tests were registered by employing non-contact Digital Image Correlation Aramis® System. The numerical computations based on finite element method by using two different discrete models were carried out to validate the empirical results. To solve the problems, true stress-logarithmic strain curves of one-directional tensile tests dependent on temperature both for considered metals and glue were implemented to software. Numerical estimations based on Green–Lagrange equations for large deflections and strains were conducted. The paper reveals the influence of temperature on the behaviour of compressed C-profile Ti-Al columns. It was verified how the load-carrying capacity of glued bi-metal column decreases with an increase in the temperature increment. The achieved maximum loads at temperature 200 °C dropped by 2.5 times related to maximum loads at ambient temperature.


1954 ◽  
Vol 100 (1) ◽  
pp. 81-88 ◽  
Author(s):  
Donald Greiff ◽  
Henry Pinkerton

A vacuum sublimation apparatus is described which will permit, (a) the removal of water from virus suspensions at temperatures ranging down to –80°C., (b) continuous operation with a minimum of attention from the investigator, (c) sealing off of samples at operating pressures (10–5 mm. Hg), (d) simultaneous lyophilization of aliquot samples at different temperatures, (e) isolation of a portion of the apparatus without disturbing the remainder of the system, and (f) determination of the end-point of sublimation without disturbing the samples. The time required for drying 0.1 ml. of influenza virus suspension was shown to increase markedly with decrease of temperature, 8 days being required for dehydration at –80°C. in contrast to 2 days at –30°C. and 1 day at 0°C.


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