514 



EXPERIMENT STATION RECORD. 



free from phosphoric acid H3PO4, possibly identical with 'paranucleic acid,' the 

 composition found for the organic part of all of these preparations is so nearly the 

 same as to show that the proteid and the nuclein are both compounds of one and 

 the same proteid body, vitellin, with a phosphoric acid, possibly H3PO4, HgPaOg, or 

 some very simple organo-phosphoric acid." 



The protein constituents of egg white, T, B. OsBorne and G. F. 

 Campbell {Connecticut State -Sta. Rpt. 1899^ pt. 3^2)^.31^8-375; Jour. 

 Amer. Chem. Soc, ^2 {1900), No. 7, jpp. 4.22-4S0).—ln a previous paper 

 (E. S. R., 11, p. 309) the author .stated that with the substance com- 

 monly called ovalbumin there is associated one or more other proteid 

 bodies, the properties of which were not definitely ascertained. The 

 present investigation, which was on a larger scale, confirms this con- 

 clusion and presents much additional information respecting these 

 other proteid bodies. 



In addition to ovalbumin the authors find in egg white ovomucin, 

 conalbumin, and ovomucoid. The properties and composition of each 

 of these bodies are described at length. Ovalljumin is the chief con- 

 stituent of egg white, constituting over 50 per cent. Ovomucin is a 

 glycoproteid and constitutes about 7 per cent of the proteid matter of 

 egg white. Conalbumin is obtained from the fractions from which 

 the proteids of egg white are obtained after separating the crystalized 

 fractions. It is separated by heating to 65"^ and is designated conal- 

 bumin "on account of its close relation in properties and composition 

 to ovalbumin. What this relation may be, we have not determined. 

 Conalbumin and ovalbumin may be different compounds of the same 

 protein, or the former may be a derivative of the latter involving a 

 molecular change." Ovomucoid, a glycoproteid, is obtained after all 

 the proteids coagulable by heat have been separated, being precipi- 

 tated by ammonium sulphate solution. The composition of these 

 proteids is shown in the following table: 



Composition vf ovomucin, ovalbumin, conalbumin, and ovomucoid. 



The purest preparations of ovalbumin, having a constant specific 

 rotation and the same composition and temperature of coagulation, 

 all gave solutions when boiled with acids which yielded considerable 

 quantities of crystalline precipitates with phenylhydrazin. The 

 amount of osozone actually obtained corresponds to from 2 to 2.5 per 

 cent of carbohvdrate calcidated as glucone. The authors discuss the 



