Dissociation of human hemoglobin by different organomercurials

The reaction of free and masked SH groups of human hemoglobin with a variety of organomercurials promotes dissociation into α and β chains which can be followed by starch-gel electrophoresis. The dissociating power depends on the position of the substituent groups with respect to the mercury although other properties such as charge and size of the mercurial may play a role. A necessary prerequisite of the mercurial in order to bring about dissociation into chains is the presence of a bulky group attached to the mercury. Perplexing phenomena observed in the behavior of hemoglobin in the presence of excess mercurial and NaCl have been explained on the basis of “symmetrization” reactions of the free organomercurial and may be of general importance whenever mercurials are used as protein reagents.