Reduction of sulfoxides in peptides and proteins Article

Houghten, RA, Li, CH. (1979). Reduction of sulfoxides in peptides and proteins . ANALYTICAL BIOCHEMISTRY, 98(1), 36-46. 10.1016/0003-2697(79)90702-4

cited authors

  • Houghten, RA; Li, CH

abstract

  • The reduction of methionine sulfoxide to methionine in peptides and proteins has been systematically investigated in terms of specific reducing agent, concentration of reducing agent, temperature, pH of the solution, and the presence of denaturing agents. While several of the reagents examined had a greater rate of reduction, N-methylmercaptoacetamide was found to be the reducing agent of choice as it was the reagent with the highest rate of reduction having no adverse interaction with other residues in peptides and proteins. Its rate of reduction increased until its concentration reached approximately 50% ( v v). Its reducing ability was relatively independent of pH changes but decreased with increases in acetic acid concentration. Using this reagent under acid, neutral, or basic conditions at a concentration of 0.7-2.8 m, methionine sulfoxide can be completely reduced to methionine in peptides and proteins at 37°C in 12 to 24 h. The sulfoxide form of S-carbamoylmethylcysteine in peptide and proteins takes approximately five times longer to reduce than methionine sulfoxide. © 1979.

publication date

  • September 15, 1979

published in

Digital Object Identifier (DOI)

start page

  • 36

end page

  • 46

volume

  • 98

issue

  • 1