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- W980147355 abstract "The chapter discusses the preparation of aconitase enzyme, which is a simplification of the alcohol fractionation method of Morrison, followed by column chromatography. In fresh extracts of heart, high activities of aconitase can usually be demonstrated without activating the enzyme. The enzyme loses activity in the course of purification and on storage in the purified form. In the presence of protecting agents, such as citrate or tricarballylate, the loss in activity is reversible. It becomes irreversible only on very prolonged storage. In the absence of protecting agents, the purified enzyme undergoes irreversible loss of activity relatively quickly. Reversibly inactivated enzyme can be reactivated by incubation with ferrous ions and a thiol. The activity of the enzyme is measured spectrophotometrically by following the disappearance of cis-aconitate at 240 mμ as a function of time. The enzyme is best stored in the presence of citrate. However under these conditions an equilibrium mixture of citrate, cis-aconitate, and isocitrate results, which interferes with the assay. Tricarballylate (15 mM) can be used as a protecting agent in place of citrate. This substance is not a substrate of the enzyme. Reactivation of the enzyme is achieved by incubation with thiomalate and ferrous ions." @default.
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- W980147355 date "1969-01-01" @default.
- W980147355 modified "2023-09-25" @default.
- W980147355 title "[6] Aconitase from pig heart" @default.
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- W980147355 doi "https://doi.org/10.1016/0076-6879(69)13010-4" @default.
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