Abstract
After prolonged treatment of hemoglobin with dilute alkali (1.8% NaOH) hematin complexes could be separated from the hydrolyzed liquid. The Fe content of these hematin complexes increased with the time of hydrolysis. Analysis of the last preparation showed the prosthetic group still in combination with prolin (and alanin). It seems, therefore, that the globin is decomposed by action of diluted alkali before its combination with the prosthetic group is dissolved.