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

Frederick Grinnell; Jonathans S. Nishimura

doi:10.1016/0005-2744(70)90188-9

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

Frederick Grinnell, Jonathans S. Nishimura

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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 language	English (US)
Pages (from-to)	150-157
Number of pages	8
Journal	BBA - Enzymology
Volume	212
Issue number	1
DOIs	https://doi.org/10.1016/0005-2744(70)90188-9
State	Published - Jul 15 1970

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General Medicine

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@article{b7aec5b9928841b3a8725f07e09ed1e5,

title = "The inactivation and dissociation of Escherichia coli succinyl-CoA synthetase by sulfhydryl reagents",

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.",

author = "Frederick Grinnell and Nishimura, {Jonathans S.}",

note = "Funding Information: The authors thank Dr. B. David Stollar for help generously given and for stimulating discussions. The support of the National Institutes of Health, U.S. Public Health Service (Grants GM AM-I3742 and GM-I7534 ) is acknowledged. One of us (F. G.) was a Pre-Doctoral Fellow of the U.S. Public Health Service (Grant I-FoI-GM-43,316-oi ).",

year = "1970",

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doi = "10.1016/0005-2744(70)90188-9",

language = "English (US)",

volume = "212",

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T1 - The inactivation and dissociation of Escherichia coli succinyl-CoA synthetase by sulfhydryl reagents

AU - Grinnell, Frederick

AU - Nishimura, Jonathans S.

N1 - Funding Information: The authors thank Dr. B. David Stollar for help generously given and for stimulating discussions. The support of the National Institutes of Health, U.S. Public Health Service (Grants GM AM-I3742 and GM-I7534 ) is acknowledged. One of us (F. G.) was a Pre-Doctoral Fellow of the U.S. Public Health Service (Grant I-FoI-GM-43,316-oi ).

PY - 1970/7/15

Y1 - 1970/7/15

N2 - 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.

AB - 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.

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

Abstract

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