168 



ELECTROCHEMISTRY 



EGG-ALBUMIN IN 0.05 N HC1. 



The slight irregularities are, save in the last observation, no 

 greater than might have arisen out of the uncertain magnitude 

 of the correction for the potential between the elements 2 and 3 

 in the gas-chain. 



These striking results have been confirmed by Rohonyi (31) 

 employing Merck's crystallized ovalbumin and Witte's peptone; 

 the following were the results obtained, the substances being 

 dissolved in JV/20 HC1 solution : 



A decided difference between the modes of combination of pro- 

 teins and an amino-acid with hydrochloric acid is thus very 

 clearly revealed. 



Manabe and Matula (17) and Blasel and Matula (2) have 

 shown that at low H+ ion concentrations a greater proportion 

 of H + is bound by serum albumin or gelatin than of Cl'. Ringer 

 (33) has confirmed this observation for albumoses, but he also 

 finds that in higher concentrations of hydrochloric acid (1 per 

 cent of albumose in 0.1 N HC1) the H + and Cl' are bound equally. 

 The same tendency is shown in the observations of Bugarszky 

 and Liebermann which are quoted above, for in the solution 

 containing the lowest proportion of hydrochloric acid to protein 

 the Cl' bound by the protein was about 20 per cent less than the 

 proportion of H + which was bound. 



It has been shown by Blasel and Matula (2) that deaminized 



