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- W2024886719 abstract "The two primary isoenzymes of transaldolase are inactivated on exposure to low concentrations (2 mm) of chlorodinitrobenzene at pH 9.0. At 23 ° the two isoenzymes show remarkably different rates of inactivation and only one, isoenzyme III, is inactivated at a significant rate. Above 30 ° both enzymes are inactivated. The Arrhenius activation energies for this process have been estimated as 105,000 cal/mole for isoenzyme I and 49,800 cal/mole for isoenzyme III. In each case complete loss of activity was observed when all four cysteine residues were dinitrophenylated. Substrate was found to protect against both inactivation and dinitrophenylation. The protection by substrate appears to be due to conformational changes which render the sulfhydryl groups less accessible to the reagent." @default.
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- W2024886719 date "1971-04-01" @default.
- W2024886719 modified "2023-10-16" @default.
- W2024886719 title "The reaction of the isoenzymes of transaldolase with chlorodinitrobenzene" @default.
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- W2024886719 doi "https://doi.org/10.1016/0003-9861(71)90236-0" @default.
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