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- W137179730 abstract "Conditions for the inactivation and reactivation of chick embryo deoxycytidylate deaminase (EC 3.5.4.12) are described. Aeration or dialysis in the absence of deoxycytidine 5′-triphosphate, MgCl2, and mercaptoethanol yields an inactive, disaggregated protein, which can be separated from residual active enzyme by Sephadex G-200 chromatography. Reversal of the inactive state can be effected by incubation of the protein with a mixture of deoxythymidine 5′-triphosphate (or deoxycytidine 5′-triphosphate), MgCl2, and mercaptoethanol. The rate of reactivation is dependent on temperature, pH, and mercaptoethanol concentration, and reactivation results in a reaggregation of the enzyme. Inactivation of the deaminase by the microsomal sulfhydryl-disulfide interchange enzyme is also reversed by the above conditions." @default.
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- W137179730 date "1968-09-01" @default.
- W137179730 modified "2023-09-29" @default.
- W137179730 title "Active and Inactive States of Deoxycytidylate Deaminase and Their Relation to Subunit Structure" @default.
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- W137179730 doi "https://doi.org/10.1016/s0021-9258(18)93223-0" @default.
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