254 THE BLOOD. 



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, 1 seem to indicate a 

 n on -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 

 nearly the same elementary composition (MICHEL) as the amorphous 

 mixture of albumin prepared from horse-serum (HAMMARSTEN and K. 

 STARKER. 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, wnich probably 

 exists only as cystine. LANGSTEIN 3 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 4 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 = 61-61.2, and by MAXIMOWITSCH on 

 the contrary () D = -47.47. 



The crystalline and amorphous seralbumin in aqueous solution give 

 the ordinary albumin reactions. The coagulation temperature of a 

 1-per cent solution poor in salts is about 50 C., but rises with the quan- 

 tity of salt. The coagulation of the mixture of albumins from serum 

 generally takes place at 70-85 C., but is essentially dependent upon 

 the reaction and the amount of salt present. Up to the present time no 

 seralbumin solution has been prepared free from mineral bodies. A 

 solution as free from salts as possible does not coagulate either on boiling 

 or on the addition of alcohol. On the addition of a little common salt 

 it coagulates in both cases. 5 



'-Halliburton, Journ. of Phyisol., 5 and 7; Hougardy, Centralbl. f. Physiol., 15, 

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



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

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



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



4 Zeitschr. f. physiol. Chem., 41. 



5 In regard to the relationship of neutral salts to heat coagulation, see J. Starke, 

 Sitzungsber. d. Gesellsch. f. Morph. u. Physiol. in Munchen, 1897. 



