The inactivation and dissociation of Escherichia coli succinyl-CoA synthetase by sulfhydryl reagents

Frederick Grinnell, Jonathans S. Nishimura

Research output: Contribution to journalArticle

7 Citations (Scopus)

Abstract

1. 1. In immunodiffusion experiments antiserum to carboxymethylated succinyl-CoA synthetase (succinate:CoA ligase (ADP), EC 6.2.1.5) reacted strongly with subunits prepared by treatment of the enzyme with merthiolate (ethylmercurithiosalicylate), but not with native enzyme. 2. 2. Various parameters of inactivation and reactivation of the enzyme in the presence of merthiolate were studied. These included the effects of pH, temperature, protein concentration and merthiolate concentration. 3. 3. Titration of succinyl-CoA synthetase with p-chloromercuri[14C]benzoate led to the binding of 4 moles of mercurial per mole of enzyme. The enzyme was dissociated by either merthiolate or p-chloromercuribenzoate into what appeared to be two different kinds of subunits.

Original languageEnglish (US)
Pages (from-to)150-157
Number of pages8
JournalBBA - Enzymology
Volume212
Issue number1
DOIs
StatePublished - Jul 15 1970

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Succinate-CoA Ligases
Sulfhydryl Reagents
Thimerosal
Escherichia coli
Enzymes
Chloromercuribenzoates
Immunodiffusion
Benzoates
Adenosine Diphosphate
Immune Sera
Temperature

ASJC Scopus subject areas

  • Medicine(all)

Cite this

The inactivation and dissociation of Escherichia coli succinyl-CoA synthetase by sulfhydryl reagents. / Grinnell, Frederick; Nishimura, Jonathans S.

In: BBA - Enzymology, Vol. 212, No. 1, 15.07.1970, p. 150-157.

Research output: Contribution to journalArticle

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