262 THE BLOOD. 



(from horse-serum) was first performed by GURBER. It crystallizes 

 with difficulty from other blood-sera (GRUZEWSKA). Even from horse- 

 serum only a portion, according to ROBERTSON 1 not more than 40 per 

 cent, of the albumin can be obtained as crystals, and it is also pos- 

 sible that the amorphous albumin, which is precipitated by ammo- 

 nium sulphate with difficulty, represents two seralbumins (MAXIMO- 

 WITSCH). According to GURBER and MICHEL it would seem that the 

 crystalline seralbumin is also a mixture, but this is disproved by the obser- 

 tions of SCHULZ, WICHMANN, and KRiEGER 2 . We know nothing as 

 to the behavior of the amorphous fraction of the seralbumin in this respect. 

 Because of the different coagulation temperatures, HALLIBURTON claims 

 the existence of three different albumins in the blood-serum, a view 

 which has been disputed by several experimenters, and recently by 

 HOUGARDY. On the other hand, the earlier investigations of KAUDER, 

 as well as the more recent work of OPPENHEIMER, S seem to indicate a 

 non-unit nature of the seralbumins, but this question is still an open 

 one. 



The crystalline seralbumin may perhaps be a combination with 

 sulphuric acid (K. MORNER, INAGAKI). The coagulated albumin obtained 

 from the aqueous solution of the crystals with the aid of alcohol has 

 almost the same elementary composition (MICHEL) as the amorphous 

 mixture of albumin prepared from horse-serum (HAMMARSTEN and 

 K. STARKE 4 ). The average composition was C 53.06, H 6.98. N 15.99, 

 S 1.84 per cent. K. MORNER, after the removal of the sulphuric acid 

 from crystalline albumin, found 1.73 per cent total sulphur, which prob- 

 ably exists only as cystine. LANGSTEIN 5 has been able to split off a nitrog- 

 enous carbohydrate (glucosamine) from crystalline seralbumin. The 

 quantity was so small that the question is still undecided whether or 

 not the carbohydrate was a contamination. The fact that ABDER- 

 HALDEN, BERGELL, and DORPINGHAUS 6 were able to prepare a seral- 

 bumin entirely free from carbohydrate and which did not respond to 

 MOLISCH'S very delicate reaction, seems to, be decisive on this point. 

 The specific rotation of crystalline seralbumins from horse-serum was 

 found by MICHEL to be (a) D = 61 to 61.2, and by MAXIMOWITSCH on 

 the contrary (a) D = -47.47. 



1 Journ. of biol. Chem., 13. 



2 In regard to the literature on the crystalline seralbumins, see Schulz, Die Kristal- 

 lisation von Eiweissstoffen, Jena, 1901; Maximowitsch, Maly's Jahresber., 31, 35. 



3 Halliburton, Journ. of PhysioL, 5 and 7; Hougardy, Centralbl. f. Physiol., 15, 

 665; Oppenheimer, Verhandl. d. physiol. Gesellsch., Berlin, 1902. 



4 Michel, Verhandl. d. phys-med. Gesellsch. zu Wurzburg, 29, No. 3; K. Starke, 

 Maly's Jahresber., 11; K. Morner, 1. c.; Inagaki, Biochem, Centralbl., 4, p. 515. 



6 K. Morner, 1. c.; Langstein, Hofmeister's Beitrage, 1. 

 6 Zeitschr. f. physiol. Chem., 41. 



