70 THE NITROGENOUS DERIVATIVES OF THE ALBUMINS. 



tive relations between the hexon bases are always the same, and as a 

 matter of fact we have reason to assume that the nucleus of most of 

 the complex albumins contains more lysin groups than are found in 

 the sturin molecule. 



As regards the further development of the complex albumins 

 from protamins, Kossel imagines that these are formed through the 

 union of a protamin radicle with various other radicles, which partly 

 belong to the class of the mo no-am ido-acids, and partly to the aro- 

 matic series, to which a sulphur or an iodine radicle can further be 

 added. These various bodies can then also combine with each other 

 or with foreign radicles to form still more complex substances. A 

 relation is thus established between the lowest forms of the albumins 

 and the carbohydrates, and just as the polysaccharides can be decom- 

 posed by hydrolysis into the hexoses, so also are the protamins trans- 

 formed into hexons. This decomposition in both instances, more- 

 over, can be effected through the agency of ferments. Diastase thus 

 causes inversion of the polysaccharides to hexoses, and trypsin can 

 similarly break down the protamins, with the formation of the hexon 

 bases. Whether a reversion is here also possible has not as yet been 

 ascertained. 



As the size of the protamin molecule has not been established, it 

 is possible only to indicate the composition of salmin, sturin, and 

 scombrin by the respective formulae (C^H^N^O^, (C 36 H 69 N 19 CX).T, 

 and (C^HeAAX 



Like the complex albumins, the protamins give the bluish-violet 

 biuret reaction, and from what has been said we have reason to 

 assume that this reaction in the case of all albumins is referable to 

 the presence of a protamin group. The xanthoproteic reaction, 

 Millon's reaction, Molisch's reaction, and the sulphur-test, on the 

 other hand, are negative. 



The aqueous solutions of the protamins are strongly alkaline ; 

 from these solutions they are precipitated by picric acid, phospho- 

 tungstic acid, iodopotassic iodide, potassium ferrocyanide in the 

 presence of acetic acid, by salting with sodium chloride or ammo- 

 nium sulphate, etc. They combine with acids to form salts, among 

 which the sulphates are especially characteristic, as on cooling^ or 

 upon the addition of ether they separate from their aqueous solution 

 in the form of an oily material. With the salts of the heavy metals 

 they further combine to form double salts. With the coagulable 

 albumins and the so-called primary albumoses, in ammoniacal solu- 

 tion, the protamins combine to form compounds which are apparently 

 identical with the histons, and are precipitated as such. Neither the 

 protamins nor their salts have thus far been obtained in the crystal- 

 line state. 1 



1 Quite recently Kunijeff announced that he has been able to isolate pro- 

 tnmins also from the mature spermatozoa of the pike, of Silurus glanis and Acci- 

 pensis stallatus. The products from the two latter he has termed rilurin and 

 acciwnwrin, respectively. For the accipenserin sulphate he gives the formula 

 C 35 H 72 N 18 O 9 .4H 2 SO 4 . He regards it as closely related to sturin. 



