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- W2091974247 abstract "Abstract A stabilizing factor, previously reported to protect phosphofructokinase (EC2.7.1.11) from thermal or lysosomal inactivation, has been shown to stabilize ATP-citrate lyase (EC 4.1.3.8) from thermal inactivation ( B. Osterlund and W. A. Bridger, 1977 , Biochem. Biophys. Res. Commun. , 76 , 1–8). We now report that this factor protects ATP-citrate lyase from inactivation by proteases extracted from lysosomes. While it has been suggested that the stabilizing factor may play a role in the turnover of other lipogenic enzymes, we have found that the factor has no stabilizing or other effects on NADP + -malic enzyme (EC 1.1.1.40). In order to assess the properties and mode of action of the stabilizing factor with regard to interaction with its target enzyme(s), the factor has been extensively purified from rat liver and characterized as to its composition. Although glutathione appears to copurify with the factor, and glutathione exerts some stabilizing effects on ATP-citrate lyase, the factor is clearly distinguishable from glutathione on the basis of its mode of action and its concentration dependence. Several other biological compounds have been tested in attempts to identify the chemical nature of the stabilizing factor. Thus, biotin, pyridoxal phosphate, glucose tolerance factor, substrates for ATP-citrate lyase, and oxidized glutathione have been eliminated as possible identities for the stabilizing factor. In contrast to results reported by other workers (who investigated stabilization of phosphofructokinase) we find this factor to be insensitive to treatment by proteases or sulfhydryl reagents when tested by its ability to protect ATP-citrate lyase from inactivation." @default.
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- W2091974247 date "1980-12-01" @default.
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- W2091974247 title "Characterization of a stabilizing factor of rat liver and of the nature of its interaction with ATP-citrate lyase" @default.
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- W2091974247 doi "https://doi.org/10.1016/0003-9861(80)90131-9" @default.
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