EXPERIMENT STATION RECORD. 



Vol. XXIX. Abstract ;N umber. No. 6. 



RECENT WORK IN AGRICULTURAL SCIENCE. 



AGRICULTITRAL CHEMISTRY— AG-KOTECHNY. 



Annual reports on the progi-ess of chemistry for 1912, edited by J. C. 

 Cain and A. J. Greenaway (Ann. Rpts. Prog. Chem. [London], 9 (1912), pp. 

 IX+3.'fJf, figs. 2). — This report deals with the progress made in general, physical, 

 inorganic, organic, analytical, physiological, agricultural, and mineralogical 

 chemistry, vegetable physiology, and radioactivity, continuing previous work 

 (E. S. E., 27, p. 616). 



Heinrich Ritthausen, T. B. Osborne {Biochem. Bui., 2 (1913), No. 7. pp. 

 335-339, pi. 1). — ^A detailed statement of the contributions of the late Prof. 

 Heinrich Ritthauseu to agricultural chemisti-y, with especial reference to pioneer 

 work in plant protein chemistry. 



Publications of Prof. Heinrich S-itthausen, L. W. Fetzer (Biochem. Bui., 2 

 (1913), No. 7, pp. 339-346) .—This is a comparatively complete bibliography of 

 his publications on agricultural and vegetable protein chemistry, embracing 138 

 titles. 



Index of Zeitschrift fiir Angewandte Chemie, compiled by B. Rassow 

 ( [Register der] Zeitschrift fiir Angewandte Chemie, Band 25, Refte 27-52. 

 Leipsie, 1912, pp. VII+2673-2S28). — This number contains the author, subject, 

 and patent index for the second part of volume 25 of this journal. 



On the " heat coagulation " of proteins. — III, The influence of alkali 

 upon reaction velocity, Harriette Chick and C. J. Martin (Jour. Physiol., 

 45 (1912), No. 1-2, pp. 61-69, fig. 1). — In this work, which is a continuation of 

 that previously reported (E. S. R., 26, p. 306), the heat coagulation of pro- 

 teins in the presence of free alkali (NaOH and MgO) was studied. The mate- 

 rial used was recrystallized egg albumin from which the ammonium sulphate 

 was removed by dialysis. 



" Denaturation-rate of egg albumin in alkaline solutions is shown to be in- 

 creased with increasing concentration of hydroxyl ions exactly as was previously 

 shown to be the case with increase of hydrogen ion concentration in acid 

 solution. Continuous removal of hydroxyl ions as denaturation proceeds takes 

 place in alkaline solution, just as in acid solution hydrogen ion concentration 

 was found to diminish. If precautions are taken to keep the concentration of 

 hydroxyl ions constant during the process, denaturation proceeds as a reaction 

 of the first order (as was also shown in the case of acid). If no such device 

 is employed, denaturation-rate does not remain proportional to the concentra- 

 tion of unchanged albumin, but departs farther and farther from this value 

 owing to the progressive fall in ' alkalinity.* 



501 



