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- W1977674347 abstract "Sulfhydryl reagents and oxidized CoA were examined for their effects on the various forms of pig heart succinyl-CoA synthetase (GDP-forming)(succinate:CoA ligase (GDP-forming), EC 6.2.1.4, also known as succinate thiokinase. Upon treating the polymorphic enzyme with mercaptoethanol or dithiothreitol, the pI 6.2 species was converted to the pI 6.0 form, indicating that the redox states of the enzyme sulfhydryl groups may be responsible for the differences in isoelectric points. Titration of the pI 6.2 and 6.0 enzymes with 5,5′-dithiobis-(2-nitrobenzoic acid) (DTNB) in the presence of sodium dodecylsulfate yielded 35.5 and 38.5 moles of sulfhydryl group per mole of enzyme, respectively. Therefore it appears that the two enzyme forms do not have greatly different sulfhydryl group contents and that only a small number, possibly one or two disulfides are reduced to free sulfhydryls by dithiothreitol in the conversion of the pI 6.2 to pI 6.0 enzyme form. Incubation of succinyl-CoA synthetase with oxidized CoA before electrofocusing resulted in the formation of two enzyme species with isoelectric points of 5.3 and 5.2; each form had the same amount of bound CoA per unit of enzymic activity. These forms were not observed when dithiothreitol was added to the incubation mixture. Also, the CoA bound to the enzyme was discharged by dithiothreitol, indicating that a disulfide compound is formed from succinyl-CoA synthetase and oxidized CoA. Both the pI 5.3 and 5.2 enzymes contained exchangeable phosphate." @default.
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- W1977674347 date "1974-01-01" @default.
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- W1977674347 title "Sulfhydryl groups, a factor in the polymorphism of succinyl-CoA synthetase (GDP-forming)" @default.
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- W1977674347 doi "https://doi.org/10.1016/0005-2744(74)90166-1" @default.
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