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Title

Enzymatic synthesis of isotopically labelled serine and tryptophan for application in peptide synthesis

Authors
Malthouse, J P
Milne, J J
Grehn, L
Ragnarsson, U
Published in Journal of Peptide Science. 1997, vol. 3, no. 5, p. 361-366
Abstract L-[1.2-13C2, 15N]Serine was prepared from [1,2-13C2, 15N]glycine on a gram scale by the use of the enzyme serine hydroxymethyltransferase. The reaction was monitored by 13C-NMR spectroscopy. This is the first simultaneously 13C- and 15N-labelled serine isotopomer so far reported. Part of the product was directly converted by tryptophan synthase to L-[1,2-13C2, 15N]tryptophan which could conveniently be purified and isolated as Boc-derivative in a yield of 71%. Most of the serine was isolated similarly but to remove remaining starting material in this case purification by column chromatography was required.
Keywords Carbon IsotopesGlycine Hydroxymethyltransferase/metabolismMagnetic Resonance SpectroscopyNitrogen IsotopesSerine/chemistry/metabolismTryptophan/chemistry/metabolismTryptophan Synthase/metabolism
Identifiers
PMID: 9391911
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MALTHOUSE, J P et al. Enzymatic synthesis of isotopically labelled serine and tryptophan for application in peptide synthesis. In: Journal of Peptide Science, 1997, vol. 3, n° 5, p. 361-366. https://archive-ouverte.unige.ch/unige:89535

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Deposited on : 2016-11-29

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