226 



VI. HEMOGLOBIN 



while small differences in the position of the bands of the native 

 protein compounds are known {cf. Chapter VII). 



Figures 2 and 3* give the absorption spectra of oxyhemoglobin, 

 carbon monoxide hemoglobin, hemoglobin, hemzglobin, and hemi- 

 globin cyanide over the whole range from the infrared (1000 m/ix) to 



500 



100 



10.0 



1.00 



0.10 



0.010 

 0.005 



900 800 700 600 500 



WAVELENGTH, m^ 



400 



300 



Fig. 2 Absorption spectra of oxyhemoglobin, hemoglobin, and hemiglobin cyanide 

 drawn from data of B. L. Horecker.* 



the ultraviolet (about 300 m/x). These have been drawn principally 

 from data kindly supplied to us by Dr. B. L. Horecker. They show 

 clearly the remarkable transparence of carbon monoxide hemoglobin 

 in the infrared, which was discovered by Eggert {61^9) and studied by 

 Matthes and Gross (1884), Sid well and co-workers (25^9), and par- 

 ticularly by Horecker {13J^3). They also show that, in addition to 

 the Soret band, hemoglobin and hemiglobin have only one band in the 

 ultraviolet (270-280 m/x), while oxy- and carboxyhemoglobins have a 

 third band in the region of 330-340 m^. Drabkin has pointed out 

 that these absorption bands in the ultraviolet are not derived from 

 globin, though modified by it. As has been mentioned in Chapter 



