Abstract
Free and masked SH groups were determined in haptoglobine (Hp) haemoglobine (Hb) (horse) and in their complex (Hb-Hp). Hp contains no free SH groups, but up to 9 groups are liberated per mol on denaturation by guanidine. The Hb-Hp complex reacts with the same number of Hg++ ions as free Hb, but it reacts with one less Ag+ ion than free Hb. The 4th Ag+ ion is taken up only in the presence of low concentration of a denaturing agent. Hg++, Ag+, Cu++ pcmb and iodine do not inhibit the association of Hb and Hp nor do they diminish the peroxidasic activity of the complex. Sh groups of Hb do not seem to be involved in these two reactions.
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