Summary
γ-Butyrobetaine hydroxylase catalyses the last step in carnitine biosynthesis, the formation of L-carnitine from γbutyrobetaine, a reaction dependent on Fe2+, α-ketoglutarate, ascorbate and oxygen. Initial attempts to purify the protein from rat liver showed that γ-butyrobetaine hydroxylase is unstable. We, therefore, determined the influence of various compounds on the stability of γ-butyrobetaine hydroxylase at different storage temperatures. The enzyme activity was best conserved by storing the protein at 4°C in the presence of 200 g/1 glycerol and l0mM DTT. We subsequently purified the enzyme from rat liver to apparent homogeneity by liquid chromatography.
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© 2002 Kluwer Academic Publishers
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Vaz, F.M., van Gool, S., Ofman, R., IJ1st, L., Wanders, R.J.A. (2002). Carnitine Biosynthesis. In: Quant, P.A., Eaton, S. (eds) Current Views of Fatty Acid Oxidation and Ketogenesis. Advances in Experimental Medicine and Biology, vol 466. Springer, Boston, MA. https://doi.org/10.1007/0-306-46818-2_13
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DOI: https://doi.org/10.1007/0-306-46818-2_13
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