Introduction of thiol-reactive structures on to soluble and insoluble proteins

Biotechnol Appl Biochem. 2000 Jun;31(3):231-7. doi: 10.1042/ba19990097.

Abstract

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acids / analysis
  • Biochemistry / methods*
  • Chromatography, Affinity / methods
  • Disulfides / chemistry
  • Enzyme-Linked Immunosorbent Assay
  • Gels
  • Immunoglobulin G / chemistry
  • Keratins / chemistry
  • Methionine / chemistry
  • Methionine / metabolism
  • Molecular Weight
  • Oxidants / chemistry
  • Oxidation-Reduction
  • Phthalic Acids / chemistry
  • Proteins / chemical synthesis
  • Proteins / chemistry*
  • Serum Albumin, Bovine / chemistry
  • Solubility
  • Sulfhydryl Compounds / chemistry*
  • gamma-Globulins / chemistry

Substances

  • Amino Acids
  • Disulfides
  • Gels
  • Immunoglobulin G
  • Oxidants
  • Phthalic Acids
  • Proteins
  • Sulfhydryl Compounds
  • gamma-Globulins
  • Serum Albumin, Bovine
  • Keratins
  • Methionine
  • magnesium monoperoxyphthalate