MEAH)li;8 OF THK NATIONAL ACADEMY OF tSClENCKS. H^i 



Xlll.— SlMMAKY OK KKSILTS.* 



1. Tlip protcid body reinovi'd iVoiii frosli prouiid oats by direct extraction with weak alcohol — 

 first observed by Norton and by him designated ijl itt in— wUvii (U'liydrat«'d by absohite alcohol and 

 dried over snlphnric aciil, is a lijrlit yellowish powder, insolnble in pure water as well as in abso 

 Iftte alcohol, solnble in niixtnres ot' ai<-oliol and water, solnble also in dilate acids and alkalies, 

 and from these sohitions thrown down by nentrali/.ation. Separated from its sohition in aholiol 

 of tit) i)er cent by evaiHiratinjr olVthe alcohol, it forms a yellowish, slimy mass. Its composition 

 (as tbund for prejjaration 8t) is given in the table, under I. This substance is remarkabh- 

 for its considerable content of sulphur, which is exceeded by that of keratin alone among the 

 proteids, and is otherwise (M|ualed only by that recorded in some analyses of serum albumin. (See 

 pp. 57-59.) 



2. When the substance described above is heated with dilute alcohol for .some time it coagu- 

 lates and becomes insoluble in that liipiid, but without apparent change of comixisition. II 

 is the average of three accordant analyses of this coagidated form of the alcohol soluble protcid, 

 made on preparations 4 A, 4 B, and 7 (pp. 65-57). 



Kreusler obtained this material from the oat, but what Ititthausen and he named oatgliadin 

 was a product of its further alteration by the chemical treatment to which it was subjected with a 

 view of purification. (See pp. 58-59.) 



3. When oats are first treated with water or 10 per cent solution of common salt, before 

 extraction with dilute alcohol, the alcohol soluble proteid undergoes alteration, and a body of 

 diflerent composition and properties residts. In the table, III, gives the mean of closely 

 agreeing analyses of this substance made on preparations 9, 10, 11, and 12; it is much more 

 soluble in dilute alc(diol than I, and is not coagulateil or transformed into an insoluble modifica- 

 tion. When wet with absolute alcohol, the moisture attracted from the air shortly renders it 

 gummy and tenaciously adhesive, unlike I (pp. 59-C3). 



Its composition as regards carbon, hydrogen, and nitrogen, is very near to that found by 

 Dumas and Cahours, and also by v. Hibra, for (jliudiii or phuit gelatin (extracted by hot alcohol 

 fi'om wheat gluten and remaining dissolved in the alcohol when cold). 



4. The chief proteid extracted by cold 10 per cent salt solution behaves towards reagents like 

 the myosin gJohulin from animal muscle, as first stated by Weyl. Contrary to Weyl's observations, 

 however, the coagulation temperature (SOO-lOO^) is much higher than that of animal myosin 

 (550-00°). This proteid appears to be the result of a transformation similar to that by which 

 myosin is formed fioni myosinogen. Its composition — the average of several analyses on prepara- 

 tions 13 and 14 — is given under IV ^table), and is very near to that of muscle myosin. The 

 greatest proportion of this proteid extracted by salt solution from the oat \yas 1.3 per cent. (See 

 pp. 05-08.) 



5. The proteid extracted, after complete exhaustion of the oats with alcohol of 0.9 sp. gr., by 

 10 per cent salt-solution (analysis of jueparation 15 under V., table ), and that dissolved out 

 by dilute potash (analysis of preparation 16 under V a), have so nearly the same composition as 

 the globulin extracted by salt-solution directly that they may be regarded as originally identical, 

 IV rejjresenting the soluble form, V and V a the insoluble or "albuminate" modification. (See 

 pp. 08-71). 



0. When ground oats are directly extracted by alkali-solutions, without previous treatment 

 with water or dilute alcolud, nearly the whole of the proteids is dissolved. The substance .so ex- 

 tracted, after comjiletely removing the body soluble in weak alcohol, is perhai)s the same as that 

 first designated avrnine by Johnston and Norton, who extracted oats with dilute ammonia-water. 

 Its composition is stated under VI and VI n. (Sec also pi*. 71-72). 



7. When gnmnd oats are exposed totlic action of water, a large share of the proteids becomes 

 insoluble in dilute potash solution, the amount so rendered insoluble increasing with the dura, 

 tion of the contact with water. One houi-'s treatment with water rendered one-half, twenty-tbui- 



"The Diimbers of the paragruiibs in this summary correspoud with the numbers over tbe analyses in the table 

 following. 



t J'ide p. 57. 



