568 H^EMATIN. [BOOK n. 



globin, though not in the exact condition in which it naturally 

 exists in the compound ; this substance when separated out 

 appears as a brownish-red body known as hcematin. All the iron 

 belonging to the ha?moglobin is in reality attached to the hpematin. 

 A solution of haemoglobin, when heated, coagulates, the exact 

 degree at which the coagulation takes place depending on the 

 amount of dilution ; at the same time it turns brown from the 

 setting free of the hsematin. If a strong solution of ha?moglobin 

 be treated with acetic (or other) acid, the same brown colour, from 

 the appearance of hamatin, is observed. The proteid constituent 

 however is not coagulated, but by the action of the acid passes 

 into the state of acid-albumin. On adding ether to the mixture, 

 and shaking, the hn -matin is dissolved in the supernatant acid 

 ether, which it colours a dark red, and which, examined with the 

 spectroscope, is found to possess a well-marked spectrum, the 

 spectrum of the so-called acid ha-matin of Stokes (Fig. 76, 6). 

 The proteid in the water below the ether appears in a coagulated 

 form owing to the action of the ether. In a somewhat similar 

 manner alkalis split up haemoglobin into a proteid constituent 

 and hsematin. 



The exact nature of the proteid constituent of haemoglobin 

 has not as yet been clearly determined. It was supposed to 

 be globulin (hence the name ha-matoglobulin, contracted into 

 haemoglobin), but though belonging to the globulin family, has 

 characters of its own ; it is possibly a mixture of two or more 

 distinct proteids. It has been provisionally named globiji and is 

 said to be free from ash. 



351. H;t -matin when separated from its proteid fellow, and 

 purified, appears as a dark-brown amorphous powder, or as a scaly 

 mass with a metallic lustre, having the probable composition of 

 C 32 , H 34 , N 4 , Fe, 5 . It is fairly soluble in dilute acid or alkaline 

 solutions, and then gives characteristic spectra (Fig. 76, 1, 2, 5). 



An interesting feature in ha-matin is that its alkaline solution 

 is capable of being reduced by reducing agents, the spectrum 

 changing at the same time (Fig. 76, 3), and that the reduced 

 solution will, like the haemoglobin, take up oxygen again on 

 being brought into contact with air or oxygen. This would 

 seem to indicate that the oxygen-holding power of haemoglobin 

 is connected exclusively with its hrematin constituent. 



By the action of strong sulphuric acid ha-matin may be robbed 

 of all its iron. It still retains the feature of possessing colour, the 

 solution of iron-free hamatin being a dark rich brownish red ; but 

 is no longer capable of combining loosely with oxygen. This 

 indicates that the iron is in some way associated with the peculiar 

 respiratory functions of haemoglobin ; though it is obviously an 

 error to suppose, as was once supposed, that the change from 

 venous to arterial blood consists essentially in a change from a 

 ferrous to a ferric salt. 



