Polarographic studies with the dropping mercury kathode. Part XLII. The salt action in the electro-reduction of nitrates

1934 ◽  
Vol 6 ◽  
pp. 339-353 ◽  
Author(s):  
M. Tokuoka ◽  
J. Růžička
Keyword(s):  
1920 ◽  
Vol 3 (2) ◽  
pp. 237-245 ◽  
Author(s):  
Jacques Loeb

1. It is shown that the NH4 ion acts in cases of antagonism on the egg of Fundulus more like the K ion than the Na ion; this corresponds to the fact that in its general chemical behavior the NH4 ion resembles the K ion more closely than the Na ion. 2. It is shown that the tolerance of sea urchin eggs towards the Li ion can be increased 500 per cent or more if at the same time a certain amount of Na ion is replaced by K, Rb, or Cs ions. Since in the periodic table Na occupies a position between K and Li it is inferred that the Li and K ions deviate in their physiological action in the opposite direction from the Na ion. 3. These data indicate that the behavior of the K ion in antagonistic salt action (which forms the basis of the physiologically balanced action of ions) is due to its purely chemical character, i.e. its position in the periodic table or rather to its atomic number, and not to those explosions in its nucleus which give rise to a trace of radioactivity.


Science ◽  
1916 ◽  
Vol 44 (1138) ◽  
pp. 574-576 ◽  
Author(s):  
J. Loeb

2014 ◽  
Vol 53 ◽  
pp. 40-47 ◽  
Author(s):  
Zhendi Wang ◽  
Qiang Zeng ◽  
Ling Wang ◽  
Yan Yao ◽  
Kefei Li

1919 ◽  
Vol 1 (6) ◽  
pp. 607-612 ◽  
Author(s):  
J. H. Northrop

1. At equal hydrogen ion concentration the rate of pepsin digestion of gelatin, egg albumin, blood albumin, casein, and edestin is the same in solutions of hydrochloric, nitric, sulfuric, oxalic, citric, and phosphoric acids. Acetic acid diminishes the rate of digestion of all the proteins except gelatin. 2. There is no evidence of antagonistic salt action in the effect of acids on the pepsin digestion of proteins. 3. The state of aggregation of the protein, i.e. whether in solution or not, and the viscosity of the solution have no marked influence on the rate of digestion of the protein.


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