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• W1521158796 abstract "This chapter discusses the reversible introduction of thiol compounds into proteins by use of activated mixed disulfides. For the preparation of synthetic mixed disulfides, equilibrium reactions are unsuitable. Instead, the thiol groups of the protein are subjected to an activation reaction yielding an activated mixed disulfide (AMD) of the protein. Because of favorable equilibrium constants, AMDs require only 1-3 equivalents of the thiol compound to be reacted. The yellow-colored thionitrobenzoate anion (TNB) anion is a convenient tool for monitoring the kinetics of the S-alkylthiolation reaction at 412 nm. For spectrophotometric control, however, the protein AMD must be separated from excess Ellman's reagent and the TNB formed during the preparation—for example, by gel filtration. The derivatization of protein thiols via activated mixed disulfides has several advantages over other derivatization procedures. First, the reaction kinetics can be followed spectrophotometrically. Second, the procedure allows introducing arbitrary residues into proteins almost independent of molecular weight, provided they are available as thiol compounds. This makes thiol-specific derivatization of proteins independent of the availability of the corresponding maleimide or alkyl iodide derivatives. In addition, residues introduced this way into a protein are linked by disulfide bridges, which can be easily cleaved under physiological conditions." @default.
• W1521158796 created "2016-06-24" @default.
• W1521158796 creator A5026966550 @default.
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• W1521158796 date "1995-01-01" @default.
• W1521158796 modified "2023-09-25" @default.
• W1521158796 title "[34] Reversible introduction of thiol compounds into proteins by use of activated mixed disulfides" @default.
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• W1521158796 doi "https://doi.org/10.1016/0076-6879(95)51139-3" @default.
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