Abstract
Commercial preparations of AdoMet are isolated from yeast, and the AdoMet has the configuration of the natural diastereoisomer at both the sulfonium pole and the methionyl substituent. However, such preparations are not only contaminated with ninhydrin-positive impurities but also with impurities which absorb light at 260 nm and do not react with ninhydrin, such as methylthioadenosine. Such UV-absorbing impurities interfere with determinations of AdoMet concentration. Synthetic methods yield AdoMet of high purity, but which is racemic at the sulfonium pole. Use of racemic preparations is undesirable for enzymatic studies because of the possibility that the unnatural diastereoisomer might interact with the enzyme. We have thus attempted to develop a method for purification of µmole quantities of AdoMet from commercial sources.
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Creveling, S.C., Krapf, E.C., Matthews, R.G. (1982). Interactions of adenosylmethionine with methylenetetrahydrofolate reductase. In: Biochemistry of S-Adenosylmethionine and Related Compounds. Palgrave Macmillan, London. https://doi.org/10.1007/978-1-349-06343-7_84
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DOI: https://doi.org/10.1007/978-1-349-06343-7_84
Publisher Name: Palgrave Macmillan, London
Print ISBN: 978-1-349-06345-1
Online ISBN: 978-1-349-06343-7
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