702 EXPEEIMENT STATION RECORD, 



behavior in water and in solutions. They conclude that " the presonce of 

 potassium chlorid in solutions containing calcium oxid and phosphoric anhy- 

 drid increases slightly the lime content of solutions in equilibrium with 

 dicalcium phosphate and monocalcium phosphate. 



" By the ' tell-tale ' method the composition of the solid phases was found to 

 be CaHP04.2H20 and CaH4(PO.)2.H20 with a region between, which was not 

 explored, where the composition of the solid was probably CanP04. 



" This result is in accord with Bassett's last determination of the ti'ansition 

 interval of CaHP04.2H20 <=± CaHP04+2H20, but is not in accord with his direct 

 determination of the comiiositions of the solid phases." 



The proportion of org"anic phosphorus to amids and other nonproteid bodies 

 in seeds, A. Parrozzani (Staz. Sper. Agr. Itah, 42 (1909), No. 10-11, pp. 890- 

 001; ahs. in Zentbl. Biochcm. ti. Biopliys., 10 {1910). No. 2-3. p. 78).— The 

 amount of amid nitrogen and the other nonproteid nitrogenous substances pres- 

 ent is proportional to the amount of organic phosphorus in the seed. The work 

 was done with maize seeds which were fully matured and from plants which 

 were variously fertilized. 



Comparative investig'ation in regard to the composition of the casein of 

 cow's and woman's milk, E. Abderhalden and L. Langstein {Ztschr. Physiol. 

 Chcm., 66 (1910), No. 1-2, pp. 8-12). — Wjth reference to whether the casein 

 from woman's milk yields on hydrolysis the same amount and ratio of amino 

 acids as the casein of cow's milk, the authors found identical results in regard 

 to tyrosin and glutaminic acid and that no glycocol could be found in either of 

 the caseins. The remaining amino acids also agreed fairly well for both caseins. 

 The findings, however, are not considered conclusive as regards the identity of 

 the caseins. 



Protein as a protective agent of the enzyms, L. Rosenthaler (Biochem. 

 Ztschr., 26 (1910), No. 1-2, pp. 9-13). — The results with 5- and a- emulsin, 

 diastase, and invertin show that protein exerts a protective action for tliese 

 enzyms against alkali and acids. The author, therefore, calls attention to the 

 analogy which may exist in the biochemical processes in the animal and 

 vegetable world. 



Further studies of the partial hydrolysis of proteids, E. Abderhalden and 

 C. P'UNK (Ztschr. Physiol. Chcm., 6-', (1910). No. 5-6, pp. .'/.36-.'/ '/ 6' ) .— The ex- 

 perimental data reported and discussed have to do with the problem of deter- 

 mining the structural formula of proteids with particular reference to the 

 utilization of the /3-naphthalinsulpho derivatives of the polypeptids for this 

 purpose. 



About lupeose and stachyose, E. Schulze (Ber. Dent. Cheni. Gesell., 43 

 (1910), No. 12, pp. 2230-223-'i). — The author shows that lupeose prepared from 

 the seed of lupines after treatment with nitric acid yielded saccharic acid in 

 addition to the other oxidation products. He was also able to produce a 

 potassium salt which had the characteristics of potassium saccharate. Accord- 

 ing to this, lupeose yields the same products as stachyose (E. S. R., 23, p. 110), 

 and as it yields about the same amount of mucic acid as does stachyose, it is 

 probably also a tetrasaccharid. T,upeose could not be brought to crystallize. 



Some peculiarities of the proteolytic activity of papain, L. B. Mendel and 

 Alice F. Blood (Jour. Biol. Chcm., 8 (1910), No. 3, pp. 177-213).— The experi- 

 ments led to the following conclusions: 



" The digestion of Witte's peptone by papain in the presence of the common 

 antiseptics, jadged by the tryptophan test, is very slow; in the presence of 

 SON, hydrolysis is rapid. The striking difference between HCN and other 

 investigated antiseptics is due to an acceleration of proteolysis by HCN. The 

 accelerating effect is not limited to the hydrolysis of 'peptone,' but is also 



