vin PRECIPITATION DUE TO REMOVAL OF SALTS 297 



very permanent, water-soluble compounds, for example, HC1.NH 2 . 

 COO(C 2 H 5 ). After removing the HC1 of this body with Ag 2 0, the 

 remaining radical soon decomposes by giving off the alcohol radical. 

 See also Chapter VI. 



This view is supported by the observation of Stewart 1 that the 

 globulins on being precipitated carry salts down with them; but 

 against Pauli's view, according to Cohnheim, is the fact that the 

 addition of albumin does not influence the electrical conductivity of 

 sodium-chloride solutions (according to Bugarszky and Libermann). 2 



On this principle globulin and sodium chloride would form the 

 compound (HC1) Globulin (NaOH) H 2 0, or more probably according 

 to the formula, Globulin + NaCl = Cl - Globulin - Na. In support of 

 this last view Pauli refers to the investigations of Spiro and Pemsel, 3 

 who showed that albumins can bind both acids and bases. 



Cohnheim has further pointed out that Pauli's view does not account 

 for the precipitation of the globulin which results from diluting its solu- 

 tion, as in this case no ions are removed, and he suggests that globulins 

 are rendered insoluble owing to their strong hydrolytic dissociation. 

 Osborne 4 has also stated that the globulin precipitation is caused by the 

 hydrogen-ions of the water, which again only means that hydrolysis 

 occurs. 



This hydrolysis we may assume 5 to be induced on the same principle 

 as is the hydrolytic decomposition of many salts of the heavy metals 

 which form clear solutions as long as they are concentrated, but which 

 on dilution at once undergo hydrolysis, forming insoluble hydrates. 



Starke 6 in 1900 found that he could obtain a substance giving all 

 the characteristic reactions of ordinary globulins by diluting white of 

 egg with ten times its bulk of water and then dialysing the solution at 

 a temperature of 75-85 C. 



There is formed by this process a substance which is quite insoluble 

 in pure water, and also in neutral salt solutions, but which, when 

 treated with very dilute alkalies, becomes soluble. Starke found after 

 adding the same amount of alkali to two identical quantities of globulin 

 that more globulin passed into solution if neutral salts were present, 

 and explained his results on the assumption that alkalies undergo 

 greater dissociation in the presence of neutral salts, and that for 

 this reason they produced a greater effect. As shown on p. 295 



1 G. N. Stewart, Journ. of Physiol. 24. 460 (1899). 



2 St. Bugarszky and L. Libermann, Pfliigers Arch.f. d. ges. Physiol. 72. 51 (1898). 



3 Spiro and Pemsel, Zeitschr. /. physiol. Chem. 33. 401 (1901). 



4 T. B. Osborne, ibid. 33. 225 (1905). 



5 Mann, Physiological Histology, 1902, p. 57. 



6 J. Starke, Zeitschr. f. Biol. 40. 419, 494. 



