146 Mr. W. Sutherland. [July 26, 



electrolysis is #H 2 01? broken out of trihydrol. It is shown how the number 

 of these in a solution is proportional to c~%, so that when they act upon the 

 whole solute c they produce an agent of amount proportional to c~k, 

 that is c», which, in the present case, acting on the residue (1— as) of free 

 HC1 keeps the amount x of combined HC1 formed. Hence, for equilibrium, 

 we have x = k (1—x) c* as in (17) and (18). If in (16) we neglect u/u and 

 put v = 1000, we find t = 0'78, that is to say, that N/1000 HC1, which 

 is just saturated with globulin, contains 78 per cent, of the H and CI ions in 

 combination with globulin, and only 22 per cent. free. The experiments of 

 Hardy, when summarised in (14), give a pretty complete insight into the 

 chemistry of HC1 globulin. 



As regards alkali globulins, the data of Hardy can be expressed by 



(1 gramme glob. diss, in 9*7 x 10~ 5 gramme equiv. NaOH) 



fM = 220 + 1/(0-0005 + 0-031^), 



( „ „ 18 x 10 -5 gramme equiv. NaOH) 



fi = 290 + 1/(0-0005 + 0-03H— 3), 



(glob. diss. in.N"H 4 OH) fi = 290 + 1/(0-00048 + 0-023?;-*). 



(19) 



We shall at first discuss only the first and third of these as characteristic 

 of NaOH and NH 4 OH. When v is infinite, the first gives //, = 2220, while 

 in the same units the standard data of Kohlrausch would give 444 for Na 

 and 1740 for OH, that is ^ = 2184. The formula gives complete dissociation 

 of the alkali globulin at infinite dilution. It is noteworthy that the first 

 term in (18) for NaOH globulin is 220, which is half of the standard value 

 for Na. It appears, then, that half the Na unites with globulin to form 

 a globulinate, which dissociates completely at all the dilutions of Hardy's 

 experiments, giving Na ions, and globulinic acid ions whose velocity is too 

 small to make itself apparent. As the OH of this half of the original NaOH 

 does not contribute to the molecular conductivity in the same way as the Na, 

 but yet appears in the conductivity at infinite dilution, we see that it joins 

 on to the globulin in a similar way to that of the other half of the NaOH. 

 The H of the globulin displaced by the Na atom must also join on to 

 the globulin in a different function. The other half of the NaOH seems 

 to combine with globulin in a way similar to that of HC1. A compound 

 such as NaGOH seems to be formed (with H and OH attached from the first 

 half of the NaOH), yielding ions NaGjf and GOHb which may be practically 

 two varieties of the globulinic acid with which the other half of the Na 

 combines. From the second of equations (19) it appears that if twice as 

 much NaOH is used as suffices to dissolve all the globulin, its molecular con- 



