ORGANS OF GENERATION. 295 



The albuminous bodies of the white of the egg belong partly to 

 the globulin and partly to the albumin group. 



The egg-globulin is, according to DILLNER, closely related to 

 serum-globulin. On diluting the white of the egg with water it 

 partly separates. It is also precipitated by magnesium sulphate. 

 The quantity of globulins in the white of the egg is on an average 

 6.67 p. m., or about 67 p. m. of the total proteids. According to 

 CORIK and BERAKD, we have two globulins in the white of the 

 egg, one coagulating at -f 57.5 C., and the other at -J- 67 C. 



Ovalbumin, or the albumin of the white of the egg. The com- 

 position of this albumin is C 52.25, H 6.9, N 15.25, and S 1.93#. 

 The ovalbumin has the properties of the albumins in general, but 

 differs from serum-albumin in the following : The specific rotary 

 power is lower a(D) = 38. Solutions containing medium 

 amounts of the albumin coagulate at -\- 56 C., irrespective whether 

 the amount of salt present is large or small. On the contrary, the 

 temperature of coagulation changes with a constant amount of salt, 

 but with variable amounts of albumin in the solution. Ovalbumin 

 is quickly rendered insoluble by alcohol. It is precipitated by a 

 sufficient quantity of nitric or hydrochloric acid, but it dissolves 

 with more difficulty in an excess of these acids than the serum -al- 

 bumin. Ovalbumin in solution, when introduced into the blood- 

 circulation, passes into the urine, which is not the case with serum- 

 albumin. 



According to GAUTIER and BECHAMP, ovalbumin is a mixture of two 

 albumins with a coagulation temperature 60-63 and 71-74 C. respectively. 

 According to CORIN and BERARD, it is a mixture of three albumins with a 

 coagulation-temperature respectively 67, 72, and 82 C. Perhaps the fact 

 has been overlooked that the coagulation -temperature of ovalbumiu is 

 changed by variable amounts of albumin in solution. 



Ovalbumin is obtained by precipitating the globulins with 

 MgS0 4 at + 20 C. and saturating the filtrate with Na 2 S0 4 at the 

 same temperature. The ovalbumin which separates is filtered, 

 pressed, dissolved in water, and freed from salts by dialysis. The 

 dialyzed solution is then evaporated in a vacuum or at 40-50 C. 

 If precipitated with alcohol, albumin becomes quickly insoluble. 



The mineral bodies of the white of the egg have been analyzed 

 by POLECK and WEBER. They found in 1000 parts of the ash : 

 276.6-284.5 grms. potash, 235.6-329.3 soda, 17.4-29 lime, 16-31.7 



