scholarly journals Spectrophotometric Determination of the CuSO4 Soret Coefficient of a CuSO4-H2O Binary Solutions System

2010 ◽  
Vol 1 (2) ◽  
pp. 73-76
Author(s):  
Ijang Rohman ◽  
Djaka Sasmita ◽  
Iip Izul Falah

A spectrophotometric technique for the determination of the CuSO4 soret coefficient of a CuSO4-water binary solutions system is described. A short column of solutions is placed between horizontal metal plates that are held at different temperatures. The subsequent changes in composition due to thermal diffusion are followed by monitoring changes of transmittance near the end of the solutions column. In water, CuSO4 diffuses to the warm compartment of column. The soret coefficient of CuSO4 0.0254 molal in water agrees with the appropriate theory, i.e. 17.60x10-3 °C-1 on the average.

Author(s):  
L. Domonkos ◽  
J. Liszi

A conductometric method is described and applied for the determination of the Soret coefficient of normal carboxylic acids in aqueous solutions in order to check a new model described in our previous papers. The Soret cell originally developed by Agar and Turner was applied with only minor modifications. The results show that the deviations between the measured and calculated Soret coefficients are lower than 2.5% except for formic acid (33% in average).


1977 ◽  
Vol 33 (5) ◽  
pp. 1359-1363 ◽  
Author(s):  
G. D. Rabinovich ◽  
M. A. Bukhtilova ◽  
V. P. Ivakhnik

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.


2018 ◽  
Author(s):  
Xhulieta Hamiti ◽  
Ilirjana Boci ◽  
Pranvera Lazo

2017 ◽  
pp. 1
Author(s):  
Nabil Bader ◽  
Monia Almaghboub ◽  
Nessma Alshelmani

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