CHEMISTRY. 



217 



salts or acids as well as the proportion of dissolved legumelin have a great effect on 

 the temperature at which coagulation takes place. Coagulated legumelin is soluhle 

 in very dilute alkalies. . . . 



"In dilute hydrochloric or acetic acid the coagulum is not soluble. By adding 10 

 per cent of sodium chlorid to solutions containing legumelin, and then acetic acid, 

 the acid compound of this proteid is precipitated, which dissolves in water to a solu- 

 tion that on neutralization gives a precipitate insoluble in water. . . . 



"Owing to the impossibility of separating legumelin from associated proteose, 

 except in a coagulated state, we have learned but little respecting its reactions. 



"In the following table we give the average of analyses which we have made of 

 coagulated legumelin from different seeds: 



Composition of coagulated leg umin from different needs. 



"Ritthausen recognized the presence of this proteid in the horse bean and pea, 

 and gave analyses of coagula obtained by boiling extracts of these seeds. These 

 analyses, however, do not agree well with each other and only in a general way with 

 ours. On account of the solubility in alkali of the heat coagulum of this proteid, he 

 did not consider it to be albumin. 



" Proteose. — As the proteose of these seeds is present in small amount and is diffi- 

 cult to obtain pure, we have not as much information respecting it as is desirable. 

 The pea appears to contain about 1 per cent, the horse bean about 0.5 per cent, and 

 the lentil and vetch evidently less. It is probable that more or less of this proteose 

 may be lost by diffusion, for 10.5 gm. of what was doubtless nearly pure proteose 

 from the pea, after solution and dialysis yielded only about 6 gm. when reprecip- 

 itated. We have obtained a few of the reactions of proteose from the pea and horse 

 bean, but no reactions of this proteid from the lentil and vetch. 



"By saturation with salt, solutions of the proteose of the pea and horse bean are 

 not precipitated, but by subsequently adding salt saturated acetic acid, a large part 

 of the pea proteose separates, while all but a trace of that from the horse bean is 

 thrown down. Nitric acid in the aqueous solutions of the pea proteose gives no pre- 

 cipitate unless the solution is previously saturated with salt, when a precipitate, 

 soluble on warming and reappearing on cooling, is given by that part of the proteose 

 precipitable by acetic acid from a salt saturated solution, while the part not thus 

 precipitable gives only a turbidity. Both these parts of the pea proteose are precip- 

 itated by copper sulphate, and give a rose-red biuret reaction. 



"The composition of the preparations from these seeds was found as follows: 



Proteose. 



