The interaction of 2,6-dichloroindophenol and protein sulfhydryl groups

Donald S. Coffey, Leslie Hellerman

Research output: Contribution to journalArticle

Abstract

The sulfhydryl proteins, d-aminoacid oxidase (EC 1.4.3.3) (porcine kidney), bovine-liver glutamate dehydrogenase (EC 1.4.1.3) and ovalbumin, all in a denatured state, and in addition, thiolated gelatin are all capable of reacting with 2,6-dichloroindophenol in a stoichiometry approaching 1 mole of indophenol per protein sulfhydryl residue. The product of this type of reaction is a protein-reduced indophenol adduct which can be oxidized by suitable electron acceptors including oxygen to a protein dye derivative. The indophenol component is bound tightly to the protein and resists removal by exhaustive dialysis. Pretreatment of the initial protein with p-chloromercuriphenylsulfonate completely inhibits the reduction and binding of the indophenol. These observations are discussed in terms of a thiol-substitution reaction to a ring of the indophenol dye, similar to the production of an S-glutathionyldichloroindophenol described in an earlier investigation in this laboratory1.

Original languageEnglish (US)
Pages (from-to)98-103
Number of pages6
JournalBBA - General Subjects
Volume100
Issue number1
DOIs
StatePublished - Apr 12 1965

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology

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