V>10 EXPERIMENT STATION RECORD. 



serum albumin; glolmlins, such as serum globulin and fibrinogen; sclero- 

 proteins, such as gelatin, keratin, etc. ; phosplio-proteins, such as vitellin, easein- 

 ogen, and casein ; conjugated proteins, and derivatives of proteins. 



Conjugated proteins are substances in which the protein molecule is united 

 to a prosthetic group, the principal subdivisions being uucleo-proteins, glueo- 

 proteiiis (mucin), and chromo-proteins (hemoglobin). The derivatives of 

 protein include meta-proteins (acid-albumin, alkali-albumin), proteoses (albu- 

 mose, globulose, gelatose, etc.), peptones, and polypeptids. 



As regards peptones, " this term should be restricted to the further products 

 of hydrolysis which differ from the proteoses inasmuch as "they can not be 

 salted out from solution and usually resemble them in giving the biuret test. 

 It has been pointed out that certain vegetable products hitherto regarded as 

 peptones do not give the biuret test. It does not appear possible to bring such 

 exceptional substances into any general classification at present. The same 

 difliculty in classifying arises in connection with certain other vegetable pro- 

 teins — for instance, those which, like gliadin, are soluble in alcohol." 



"The term caseinogen should be used for the principal protein in milk and 

 casein for its derivative, which is the result of the action of rennet. 



"The two principal proteins of the muscle plasma should be termed para- 

 myosinogen and myosinogen ; the term soluble myosin should take the place of 

 von Furth's soluble myogen-flbrin ; the term myosin should be restricted to the 

 final product formed during rlfior mortis." 



The chemistry of the protein bodies of the wheat kernel. II, Preparation 

 of the proteins in quantity for hydrolysis, T. B. Osborne and I. F. Harris 

 {Amer. Jour. PlnisioL. 11 U'.)06). Xo. 3. pp. 2.23-230). — Continuing earlier work 

 (E. S. R., l(j, p. 84G), the authors prepared in quantity specific proteids of 

 wheat which they had isolated, namel.v, globulin, gliadin, and glutenin. The 

 amounts of globulin obtained were not sufficient for extended study, and no 

 attempt was made to prepare the proteoses for further investigation, " as we 

 have no means of determining the origin of these proteoses or of separating 

 the mixture into products of probable chemical individuality." 



As shovA'u by an average of 25 aual.yses wheat gliadin contained 52.72 per 

 cent carbon, 6.8G per cent hydrogen, 17.66 per cent nitrogen, 1.14 per cent sul- 

 ])Iiur. and 21.62 per cent oxygen. Leucosiu and glutenin had practically the 

 same elementary composition as wheat gliadin, as did also the gliadin of rye. 

 The authors believe, however, that glutenin and gliadin are distinct bodies. 



The chemistry of the protein bodies of the wheat kernel. Ill, Hydro- 

 lysis of the wheat proteins, T. B. Osijokne and S. H. Clapp (Amer. Jour. 

 Physiol., 11 (lyoG), No. 3, pp. 2^i-26".5).— Studies of the cleavage products of the 

 specific proteids of wheat are reported from which the authors conclude that 

 gliadin, glutenin, and leucosiu are separate and distinct bodies. Gliadin is free 

 from glycocoll, the 0.(72 per cent found in one case being regarded as due to 

 the presence of a trace of glutenin. Leucosiu is similar in its composition to 

 animal proteids, which perhaps has a bearing ui)on its occurrence in the wheat 

 embryo in distinction to gliadin and glutenin, which are typical reserve pro- 

 teids. Reference to earlier work is given al)ove. 



Studies on the ti-ue nature of gluco-proteins and leucins, L. Hugounenq 

 and A. Mokel {Bui. 8oc. Cliim. France, 4. ser., 1 (1901), No. 4, pp. 154-165).— 

 Studies of the cleavage products showed that so-called leucins and gluco- 

 proteins ai'e mixtures of amido acids. 



On the increase in weight in the hydrolysis of casein, J. II. Lomg {Jour. 

 Amer. Chem. t^oc, 20 (I'JOl), No. 3. pp. 2<Jo-2'JD).— The author investigated 



