602 ORGANS OF GENERATION. 



rence of several globulins in the white of the egg there are the determina- 

 tions of CORIN and BERARD as well as of LANGSTEIN/ but they have 

 not led to any positive conclusions. 



Ovalbumin. The so-called albumin of the egg-white is undoubtedly 

 a mixture of at least two albumin-like proteins. Opinions differ con- 

 siderably in regard to the number of these proteins (BONDZYNSKI and 

 ZOJA, GAUTIER, BECHAMP, CORIN and BERARD, PANORMOFF, and others). 

 Since HOFMEISTER has been able to prepare ovalbumin in a crystalline 

 form, and since HOPKINS and PiNKUs 2 have shown that not more than 

 one-half of the ovalbumin can be obtained in such a form, OSBORNE and 

 CAMPBELL have isolated two different ovalbumins or chief fractions; 

 the crystallizable they call ovalbumin and the non-crystallizable con- 

 albumin. The two fractions have only a slight variation in elementary 

 composition; the conalbumin coagulates between 50-60 C., nearer to 

 60 C., and the ovalbumin at 64 C. or at a higher temperature. There 

 are no conclusive investigations as to whether the non-crystallizable 

 conalbumin is a mixture or not, and the question concerning the unity 

 of the crystallizable ovalbumin is also disputed. According to BOND- 

 ZYNSKI and ZOJA, crystallizable ovalbumin is a mixture of several albumins 

 having somewhat different coagulation temperatures, solubilities, and 

 specific rotations, while HOFMEISTER and LANGSTEIN on the contrary 

 believe that crystallizable ovalbumin is a unit. The reports as to the 

 specific rotation of the different fractions unfortunately differ, and the 

 elementary analyses have also given no positive results, as a variation 

 of 1.2-1.7 per cent has been observed in the quantity of sulphur. Accord- 

 ing to the consistent analyses of OSBORNE and CAMPBELL and of LANG- 

 STEIN, the conalbumin contains about 1.7 per cent sulphur and about 

 16 per cent nitrogen, while the ovalbumin contains on an average about 

 15.3 per cent nitrogen. LANGSTEIN 3 obtained 10-11 per cent glucosa- 

 mine from ovalbumin and about 9 per cent from conalbumin. The 

 ovalbumin, like the conalbumin, has the properties of the albumins in 

 general, but differs from seralbumin in the following: The specific rota- 

 tion is lower. It is quickly made insoluble by alcohol and is precipitated 

 by a sufficient quantity of HC1, but dissolves in an excess of acid with 

 greater difficulty than the seralbumin. The products isolated by ABDER- 



1 Langstein, Hofmeister's Beitrage, 1; Eichholz, Journ. of Physiol., 23; Osborne 

 and Campbell, Connecticut Agric. Exp. Station, 23d Ann. Report, New Haven, 1900; 

 Dinner, Maly's Jahresber., 15; Corin and Berard, ibid., 18. 



2 Hofmeister, Zeitschr. f. physiol. Chem., 14, 16, and 24; Gabriel, ibid., 15; Bond- 

 zynski and Zoja, ibid., 19; Gautier, Bull. Soc. chim., 14; Be"champ, ibid., 21; Corin 

 and Berard, 1. c.; Hopkins and Pinkus, Ber. d. d. chem. Gesellsch., 31, and Journ. of 

 Physiol., 23; Osborne and Campbell, 1. c.; Panonnoff, Maly's Jahresber., 27 and 28. 



3 Zeitschr. f . physiol. Chem., 31. 



