238 
PANCREATINUM. 
Hedin, S. G. (from J. of Physiol., 1905, v. 32, p. 468), reports some 
experiments with tannin and trypsin to determine the activity of the 
latter. — Biochem. Centralbl., 1905, v. 4, p. 268. 
Ehrenreich, M. (Arch. f. Verdauungs Krankh, Berlin, 1905, v. 40) 
discusses the unity and specific nature of pancreas trypsin. — Refer- 
ence from J. Am. M. Ass., 1905, v. 45, p. 1450. 
Bergell and Schiitze report that they were unable to produce an 
antiserum by injecting pancreatin solutions into rabbits or goats. 
While these preliminary experiments are not considered to be con- 
clusive, the authors appear to think that it will be impracticable to 
form antibodies for such ferments as possess peptid-binding proper- 
ties. — Chem. Centralb., 1905, v. 76, p. 154. 
PARALDEHYDUM. 
Riedel’s Berichte points out that the requirements of the Pli. 
Germ. IT, for a boiling point of from 123° to 125° was found to 
be practically correct for the ordinary variation in barometric pres- 
sure. The experiments recorded vary from 122.8° C. at 722 mm. pres- 
sure to 126.3° at 792 mm. pressure, indicating that the lower tempera- 
ture given by the U. S. P., VIII, is rather too low. — Riedel’s Berichte, 
Berlin, 1905, p. 50. 
Kebler, Lyman F., reports finding a sample of paraldehyde contain- 
ing 0.533 per cent of nonvolatile matter and congealing at 10° C. in 
place of near 0° as required by the U. S. P. VIII. — Proc. Am. Pharm. 
Ass., 1905, v. 53, p. 188. 
PEPSINUM. 
Schrumpf, P., outlines the preparation of pepsin by subjecting the 
mucous membrane of the pig’s stomach to pressure, as in Buchner’s 
work on yeast, and the liquid filtered through a Chamberlain filter. 
The pepsin separated from this filtrate by the cholesterol method 
was protein free. In some cases the solution had rennetic properties, 
in other cases not, a fact which tells against the view of Pawlow and 
Nencki that pepsin and rennin action are both due to the same mole- 
cule.— J. Chem. Soc., Lond., 1905, v. 88, part 2, p. 556. 
Bickel, Adolph (Dtsch. Med. Wchnschr., 1905, p. 1383), demon- 
strates that pepsin is quite resistant to low temperatures and that 
even so low a temperature as liquified air does not materially impair 
its activity. — Apoth. Ztg., 1905, v. 17, p. 727. 
Lucas, E. W. (Pharm. J., Lond., v. 19, p. 376), discusses the 
determination of the digestive power of pepsin and suggests a modi- 
fication of the official process. He points out that coagulated egg- 
white rubbed through a sieve is not sufficiently broken up and that 
