Thermodynamics of binding of configurationally different iron(III) complex ions by sodium dextran sulfate in aqueous solution

1980 ◽  
Vol 84 (1) ◽  
pp. 24-28 ◽  
Author(s):  
B. Pispisa ◽  
S. Paoletti
Biopolymers ◽  
1976 ◽  
Vol 15 (11) ◽  
pp. 2219-2226 ◽  
Author(s):  
M. Branca ◽  
M. E. Marini ◽  
B. Pispisa

1977 ◽  
Vol 55 (16) ◽  
pp. 2274-2277 ◽  
Author(s):  
J. H. Tremaine ◽  
W. P. Ronald

Southern bean mosaic virus (SBMV) and sowbane mosaic virus (SoMV) were each dissociated into RNA and protein components in neutral pH buffers containing ethylenediaminetetraacetic acid and 1 M NaCl. The assembly of SBMV particles and of SoMV RNA in SBMV protein was accomplished by dialysis of the virus components into low molarity buffers containing divalent metal ions. Some of these particles were stable in 1% sodium dodecyl sulfate (SDS) and had sedimentation and electrophoretic properties identical with untreated virus. Spherical particles were also assembled with either SBMV or SoMV RNA in SoMV protein and with sodium dextran sulfate in either SBMV or SoMV protein, but these particles were not stable in 1% SDS.


As early as 1853 Hittorf (‘Pogg. Ann.,' vol. 89, 181, 1853), discussing the results of his experiments, emphasised the fact, that a more detailed study of the movements of the ions during electrolysis would result in an increased knowledge of the constitution of salts in solution. He himself, in a research extending over a number of years, ( ibid ., 89, 177, 1853; 98, 1, 1856; 106, 337 and 513, 1859,) determined the ratio of the velocities of the two ions for a large number of salts, and the series of measurements has been further extended by later investigators. (For the original literature on transport number determination, see Bein, 'Zeitschrift fur Phys. Chemie,' vol. 27, 1 (1898)).


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