We have isolated calpromotin, a protein reported abundant in human red cell
s and shown to be of significance for KCl transport. We show that calpromot
in is identical to a radical scavenger protein, thiol-specific antioxidant
protein (TSA). Calpromotin is known to exist partially as a large complex o
f identical subunits and partially as dimers probably held together by disu
lfide bridges. The stability of the high-molecular-weight form was studied
by variations of pH and urea concentration. It is shown that the equilibriu
m between the large complex and the dimeric subunit is governed by the diss
ociation of a group with a pK value of about 7.5. Dissociation of the compl
ex was also complete at 2.5 M urea, where no unfolding of the peptide chain
s was detectable. (C) 1999 Academic Press.