1906.] The Chemistry of Globulin. 151 



is most probable that the internal salt formation goes on in such a way that 

 COOH and NH 2 neutralise one another.* Thus in the extreme case of all the 

 oxygen existing as COO in C12H19N3O4, two-thirds of the total nitrogen 

 would be present as NH 2 joined up with COOH in the globulin molecule. 

 When the globulin molecule is made an ion, it has probably only two COO 

 radicles showing the acid character. Hence we infer from our discussion of 

 Hardy's conductivity measurements that the globulin molecule contains NH 2 

 eight times in such a form that HC1 can join on as it does with NH 3 to form 

 OTUCl. These eight NH 2 and the two COOH are the only ones left free out 

 of about 290 of each sort existing in the globulin molecule. By more or less 

 drastic treatment the latent NH 2 and COOH radicles may be called into 

 partial action, and so globulin and albumin may be made to show apparently 

 higher acidity and basicity than the eight and the two determined above. In 

 the same way arise the discrepant results of different experimenters, discussed 

 in Section 3, as to the percentage of heavy metals in their compounds with 

 albumins. Different treatments open out or break up the albumin molecule 

 differently. But yet a rather striking agreement appears in these discordant 

 results if we regard them in the following way. The range in the percentages 

 of Cu in albuminates and globulinates is 0*45 in Mellanhy's globulinate, 

 0*71 in the albuminate of Chittenden and Whitehouse, 1*2 Morner, T35 

 Harnack, 1*85 Morner, 2*19 Chittenden and Whitehouse, 2*64 Harnack, and 

 11, the average of Eitthausen's measurements with vegetable albumins. For 

 the weight of proteid combined with a gramme equivalent of Cu (31-6) these 

 give the numbers — 



7020 4450 2630 2340 1710 1440 1200 287 

 241 15-3 9-05 8-04 5'87 4'96 410 0'987 



which are expressed in the second row as multiples of 291, these multiples 

 being all nearly exact integers 1, 4, 5, 6, 8, 9, 15, and 24. Here, then, 

 we have evidence of the splitting up or opening out of the albumin 

 molecule into parts, each of which contains an integral number of a group 

 whose molecular mass is about 291, which is quite close to the 270 of our 

 Ci 2 H 20 N 3 O4. This group with H 2 would give 288. This seems a fairly 

 conclusive proof that there is a large amount of internal salt formation in 

 albumins. The 3300 found in Section 3 for the mean mass of albumin combined 

 with an equivalent of heavy metal in Chittenden and Whitehouse's experi- 

 ments represents about 12 of our groups. It is interesting to note that 

 the treatment of a vegetable albumin with copper breaks up the albumin 

 molecule into parts of about the size of a peptone molecule. This probably 

 # See Mann, 'Chemistry of the Proteids/ pp. 210 and 211. 

 VOL. LXXIX. — B. N 



