Time. Acid added to show trace of free acid. February 6, 11.30 A.M. " 2.15 P.M. 4.5 c.c., 0.2 per cent. HCl. " 5.00 P.M. 1.0 " " " " February 7, 8.45 A.M. 3.0 " " " " " 2.00 P.M. 1.0 " " " " " 5.00 P.M. 1.5 " " " " February 8, 8.30 A.M. 1.0 " " " " " 2.30 P.M. 0.0 " " " " February 9, 8.30 A.M. 3.0 " " " " February 10, 9.30 A.M. 2.0 " " " " ---- 17.0 From these results several interesting conclusions may be drawn, in conformity with the statements already made. Thus, as soon as proteolysis commences, the products formed begin to show their greater affinity for acid by withdrawing acid from its combination with the native proteid, a supposition which is necessary to account for even the starting of the proteolytic process. Further, it is evident that proteoses and peptones combine with a far larger equivalent of acid than the native albumin is capable of; 17 c.c. of 0.2 per cent. HCl being required in the above experiment to satisfy the greater combining power of the newly formed products. This doubtless depends upon the cleavage of the large proteid molecule into a number of smaller or simpler molecules, each of the latter, perhaps, combining with a like number of HCl molecules. This view of the relationship of the individual proteoses and peptones is one more or less generally held, and is supported by many facts.[106] However this may be, it is evident that the products of pepsin-proteolysis combine with a larger amount of hydrochloric acid than the mother-proteid, and that the transformation of the latter, at least under the conditions of this experiment, is a slow and gradual process. In the living stomach, on the other hand, where the secretion of acid is progressing with ever-increasing rapidity, it is easy to see that the process of proteolysis would naturally be much more rapid. [106] See Gillespie: On the Gastric Digestion of Proteids. Journal of Anatomy and Physiology, vol. 27, p. 209.