AGRICULTURAL CHEMISTRY. 907 



tbo addition of one part couceutrated hydrochloric- acid to tive parts of that 

 filtrate. 



" Physically the new protein possesses a brown varnish-like luster which when 

 pulverized is changed into a whitish appearance. In water it swells and takes 

 on a whitish appearance. 



" When added to milk a i)art of the casein is difiested in the same. Digestion 

 is most favorable in neutral milks (>'\ i)r(ilong('d standing. 



" Physiologically the enzyniic properties are most active at a temperature of 

 05° C. At .S0° C. the ferment was destroyed. 



"The filtrate obtained after the removal of the new protein also has digestive 

 properties. 



"The influence of chemicals and sterilization tend to slightly modify the 

 soluble nitrogen compounds of the milk. 



"The addition of digestive bacterial cultures to sterilized milk in the pres- 

 ence of chloroform caused proteolysis. 



" The decomi)()sition products formed in the presence of the new protein are 

 similar to those formed in the presence of galactase and bacterial enzyms under 

 the same conditions. From these facts it is believed that the characteristic 

 digestion of the new protein and galactase are of bacterial origin. 



" The enzymic property of the new protein is one of incorporation," 



Hydrolysis of hordein, A. Kleinschmitt {Hyclrolyse cles Hordcins. Inaug. 

 DUs. Univ. Jlcidclbcrg, 1907, pp. 3.3; ahs. in Biochcm. ZcnfbJ., 7 (1908), A'o. 21- 

 22, p. SO.'t). — Hordein, the chief protein of barley, differs from other known 

 products, according to the author's conclusions, but is closely related to both 

 gliadin and zein, being midway between the two in its characteristics. 



The article contains data on the cleavage products obtained from hordein by 

 germination as compared with those of acid cleavage. 



A reaction distinguishing phosphoprotein from nucleoprotein and the 

 distribution of phosphoproteins in tissues, R. H. A. Plimmkk and F. H. 

 Scott (Jour. Chcm. Soc. [London], 93 (1908), No. 5.52, pp. 1699-1721) .—Accord- 

 ing to the authors the results of their experiments show that " phosphoproteins 

 may be distinguished from nucleoi)roteins by the action of 1 per cent sodium 

 hydroxid at 87° for 24 to 48 hours ; the phosphorus is completely separated in 

 this time as inorganic phosphoric acid. 



" Phosphoproteins are present in milk, egg yolk, and in the ova of fishes, that 

 is, in the substances which constitute the food stuffs of the embryo bird and fish 

 and the yotnig mammal. 



"A small quantity of phosphoprotein is present in the pancreas." 



A modification of the character of gluten in the presence of sulphurous 

 acid, J. DUGAST (Coinpt. Rend. Acad. »S'r/. {Paris:], tJ,G (1908), No. 2), pp. 1287, 

 1288). — The author concludes that sulphurous-acid gas produces a great change 

 in the cliaracter of gluten and modifies its baking qualities. 



The constitution of starch, Z. Gatin-(Jruzkwska (Compt. Rend. Soc. Biol. 

 [Z'ari.s], UJ^ (1908), No. /,. pp. 178, 179; ab.s. in Jiiorhcm. Znitbl., 7 (t90S), No. 

 21-22, p. 765). — The addition of concentrated potassium hydroxid solution and 

 a little alcohol to warm starch paste caused a precipitate which is identical 

 with the aniylopectin of other investigators. From the filtrate another body was 

 isolated, called by the author aniylcm, which is soluble in water. The pi'operties 

 of these bodies were studied. I'revious work has been noted (K. S. R., 20, p. 

 110). 



Further studies on the forms of milk sugar, C. S. Htdson (Jour. Amcr. 

 Chcm. Soc, 30 (ID08). No. 11. pp. 1767-1783. figs. 2).— The solubility relations 

 of milk sugar, the vapor pressures of saturated solutions of hydrated milk 

 S2304— No. 10—09 2 



