When proteins containing disulphide groups were oxidized with magnesium mon
operoxyphthalate at acidic pH, they acquired the property of binding thiol
compounds. This was the case with the insoluble protein keratin, chosen for
having a large number of disulphide bridges, and with soluble ones like BS
A and immunoglobulins. The potential applications of some of these modified
proteins for the preparation of soluble bioconjugates have been explored.
As a particular example of an application, the immobilization of activated
IgG on to solid phases might provide a new way for preparing immunoadsorben
ts.