bromochloroacetic-acid and magnesium-monoperoxyphthalate

When proteins containing disulphide groups were oxidized with magnesium monoperoxyphthalate 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 BSA 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 immunoadsorbents.

Topics: Amino Acids; Biochemistry; Chromatography, Affinity; Disulfides; Enzyme-Linked Immunosorbent Assay; gamma-Globulins; Gels; Immunoglobulin G; Keratins; Methionine; Molecular Weight; Oxidants; Oxidation-Reduction; Phthalic Acids; Proteins; Serum Albumin, Bovine; Solubility; Sulfhydryl Compounds