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

✍ Scribed by J. Paul G. Malthouse; Teresa B. Fitzpatrick; John J. Milne; Leif Grehn; Ulf Ragnarsson

Publisher: John Wiley and Sons
Year: 1997
Tongue: English
Weight: 102 KB
Volume: 3
Category: Article
ISSN: 1075-2617
DOI: 10.1002/(sici)1099-1387(199709)3:5<361::aid-psc112>3.0.co;2-o

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✦ Synopsis

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.

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