SALTS OF ALBUMIN AND ACIDS 



61 



albumin. The strong tendency to ionisation of the glutin 

 chlorides is indicated by the fact that even with an acid con- 

 centration of 0-05 N the dissociation of the protein salt is not 

 notably suppressed. Glutin chloride thus approaches some- 

 what closely to ammonium chloride in its properties. 



Table 19 (Fig. n). 

 Glutin (i per cent.) + HC1. 



The results of varying the protein content with a constant 

 concentration of acid can now be better understood. It is 

 clear that, at a low concentration of albumin, with a given 

 content of acid, relatively more H- ions will be combined than 

 when more albumin is present, owing to the fact that up to a 

 point excess of acid favours the combination of the H' ions 

 (curve H, Fig. 12). Further, as the combination of the Cl' 

 ions always lags behind that of the H' ions, the absolute 

 quantity of combined Cl' ions gradually rises to a maximum 

 with increasing concentrations of protein, and then rapidly 

 decreases (see curve II., Fig. io). 



Table 20 (Fig. 12). 

 Serum Albumin (various concentrations) -f- 0*02 N HC1. 



