Reduction of disulfide bonds in proteins by 2-aminothiophenol under weakly acidic conditions

Yoshito Abe, Tadashi Ueda, Taiji Imoto

Research output: Contribution to journalArticle

5 Citations (Scopus)

Abstract

We developed a method for reducing disulfide bonds in proteins under weakly acidic conditions by use of 2-aminothiophenol. The disulfide bonds in hen egg-white lysozyme, ribonuclease A, and soybean trypsin inhibitor were quantitatively reduced by 2-aminothiophenol in phosphate buffer, pH 6, containing 8 M Gdn HCI, 1 mM EDTA, and 20% ethanol, for 60 min at 40°C. On analysis of the RP-HPLC patterns of tryptic peptides, which were derived from reduced and S-alkylated lysozyme and ribonuclease A at pH 6, it was confirmed that no side reaction occurred. Moreover, the reduction under weakly acidic conditions was demonstrated to be applicable for the location of such a labile residue as O-acetylated tyrosine.

Original languageEnglish
Pages (from-to)52-67
Number of pages16
JournalJournal of Biochemistry
Volume115
Issue number1
DOIs
Publication statusPublished - 1994

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology

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