Summary
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1.
N-ethylmaleimide-32-pyruvate carboxylase, an enzymatically active species obtained by modification of native chicken pyruvate carboxylase with N-ethylmaleimide (Palacian andNeet [1972] Biochim. Biophys. Acta 276, 297–312), is inactivated in the cold, 0–5°, and this inactivation is accompanied by dissociation to monomers. Unlike the native enzyme, reactivation and reconstitution of the tetrameric structure upon rewarming requires the presence of ATP.
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2.
Cold inactivation of pyruvate carboxylase seems to be independent of any modification of the sulfhydryl groups of the enzyme since the sulfhydryl compound DTE (2,3-dihydroxy-1,4-dithiolbutane) has no effect on the inactivation process.
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Abbreviations
- DTE:
-
2,3-dihydroxy-1,4-dithiolbutane
References
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Palacian, E., Neet, K.E. Pyruvate carboxylase cold inactivation and sulfhydryl groups. Mol Cell Biochem 3, 35–38 (1974). https://doi.org/10.1007/BF01660075
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DOI: https://doi.org/10.1007/BF01660075