Optically pure L-valine was labelled with tritium by the Wilzbach method. Only 4 of the activity of the radiochemically pure valine was found in D-valine. This figure was determined by reverse isotope dilution. The suitability of this method for valine was tested, wich good results, with DL-valine
Tritium labelling of amino-acids and peptides by the Wilzbach method. II. Racemization of amino-acids during exposure to tritium gas
β Scribed by J. H. Parmentier
- Publisher
- John Wiley and Sons
- Year
- 1966
- Tongue
- French
- Weight
- 377 KB
- Volume
- 2
- Category
- Article
- ISSN
- 0022-2135
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β¦ Synopsis
Optically pure amino-acids were labelled with tritium by the Wilzbach method. The percentage of radioactivity found in the opposite enantiomer was determined by reverse dilution analysis. After tritiation of L-phenylalanine, D-phenylalanine, L-tyrosine, L-proline, D-proline, L-glutamic acid and L-alanine respectively 2.7, 2.2, < 1.1, 4.6, 4.0, 11.9 and 19.3 of the acticities of the radiochemically pure amino-acids were found in D-phenylalanine, L-phenylalanine, D-tyrosine, D-proline, L-proline, D-glutamic acid and D-alanine.
Wilzbach labelling of phenylalanine caused the formation of a considerable amount of a radiochemical impurity that was identijied as P-cyclohexylalanine.
π SIMILAR VOLUMES
## Abstract Ligandβexchange chromatography is shown to be applicable for obtaining the optical isomers of [^3^H]valine. Data are presented showing the effect of the asymmetric sorbent's structure on its kinetic properties and the optimum conditions selected for the chromatographic resolution of D,