The Effects of Sails on Haemoglobin 



Formula 3 is less exact than formula 1, but it is more easily applied 

 to experimental data in the form now available. 



Table I 



Ox Carbon monoxide Haemoglobin. Dialysate NaCl 0-10 M, Na 2 HP0 4 

 0-015 M, NaH 2 P0 4 0-005 M. Ionic Strength 0-15. C0 2 in solution 



after dialysis 0-0003 M. 

 •k (Osmotic pressure) 395 mm Hg at 1-0°C. E (membrane potential) 

 - 0-9 millivolts at 1-0°C .m p (protein molality) 0-007548 (36-649 g protein 



in 100 ml solution). 



The measurements summarized in Table I show the effects of a high 

 concentration of haemoglobin, comparable with the red blood 

 corpuscle, on the membrane equilibrium of sodium, chloride and 

 phosphate ions. 



In systems of this type, the differences m a — m° are directly pro- 

 portional to m p if m° be kept constant. In practice it may be essential 

 to use a high concentration of protein to obtain differences that are 

 significant. 



Some of the properties of haemoglobin in the medium specified in 

 Table I are as follows — The membrane potential E and the net charge 

 were both negative, the valence being — 1-4 for a molecular weight of 

 67,000. The isoelectric pH, where E = 0, was estimated as 6-9 ± 0-15. 

 The number of hydrogen ions combined per molecule of haemoglobin 

 was + 4-0, and the isoionic pH, where b H — 0, was estimated as 

 7-7 ±0-15 for 1-0°C. This figure is appreciably higher than most 

 published values. The correction term e t in formula 4 was estimated 

 as 0-00022 molal from the membrane potentials. The activity ratio 

 a H la° H for hydrogen ions was 1-039. 



The differences between the charge and the number of hydrogen 

 ions combined suggests that anions are associated with the protein. 



185 



