E. M. JOPE 



fractionation of the globin soluble at pYL 7-4 with 50 per cent saturated 

 ammonium sulphate the globin remaining soluble shows the tryptophan 

 band still at 290-0 m(j., but on recombination with haem this shifts 

 to 290-6 mn, much closer to the native haemoglobin wavelength of 

 291-0 mjjL. Moreover the HbCO Soret band from this fractionated 

 recombined material lies at 418 m^, again closer to the native 420 m\x. 

 But the Hb0 2 Soret band appears at 411 mfx, perhaps because of the 

 effect of the ferrous tartrate necessary to produce Hb for combination 

 with 2 . (This product probably resembles the first intermediate 

 denaturation state discussed above, p. 208.) These details supplement 

 those summarized by J. Wyman 38 . This recombined haemoglobin 

 must then be approaching the original haemoglobin in its properties 

 and it is hoped to study it further. It appears possible to prepare a 

 recombined haem-muscle globin very closely resembling the original 

 muscle haemoglobin 39 . 



Such methods as those described here and those used by Thorell 17 ' 31 

 for working with individual red cells, when based upon an adequate 

 study of the spectral absorption of the compounds involved, seem to 

 show some promise of diagnostic value in haematology as well as 

 illuminating biochemically the inter-relationships of nucleic acid, 

 protein and haem in the natural process of haemoglobin production. 

 The immediate problems are largely technical — the development of 

 sufficiently powerful sources of continuous spectrum in the ultra- 

 violet and the building of more reflecting microscopes of adequate 

 performance. These matters are receiving attention and meanwhile 

 considerable advances can be made with existing resources. A more 

 detailed account of the micro-spectroscopic methods used in the 

 above work (pp. 213, 214) is being published. 40 



/ wish to thank the Medical Research Council for a personal grant, 

 Dr E. R. Holiday for continual interest and discussion throughout this 

 work, Mr J. R. P. O'Brien for help in the earlier part of the work, 

 Dr R. Barer for work with the reflecting microscope, Dr Kuhn for 

 aluminizing its surfaces, my wife for discussion and for materials, 

 Mr M. W. Rees and Mr K. Schmid for muscle haemoglobins, the 

 Bernhard Barron Memorial Research Laboratory, Queen Charlotte' 's 

 Hospital, the Obstetrics Department, the London Hospital, and Professor 

 J. D. Boyd for supplies of human foetal blood, Mr J. C. Kendrew for 

 sheep foetal haemoglobin, Mr E. A. Johnson for help with illustrations, 

 and Mr T. Hudson for technical assistance. 



Received October 1948 



218 



