## Abstract (3,4‐^13^C~2~)‐L‐proline and (^15^N)‐L‐proline were prepared from the correspondingly labeled L‐glumatic acids via a single scheme in high yield and on a gram scale. The synthetic route is based on the ring closure of L‐glutamic acid to L‐5‐oxoproline and the selective reduction of the
Synthesis of isotopically labelled glycyl-L-prolyl-L-glutamic acid (Glypromate®) and derivatives
✍ Scribed by Paul W. R. Harris; Margaret A. Brimble
- Publisher
- John Wiley and Sons
- Year
- 2006
- Tongue
- French
- Weight
- 161 KB
- Volume
- 49
- Category
- Article
- ISSN
- 0022-2135
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✦ Synopsis
The related tripeptides glycyl-l-prolyl-l-glutamic acid (GPE) and glycyl-l-2methylprolyl-l-glutamic acid (G-2-MePE) were labelled with commercially available [1,2,3,4,5-13 C 5 , 2-15 N 1 ]-l-glutamic acid in 3 steps in excellent overall yield with high isotope incorporation. A related cyclic dipeptide was labelled with [2,2-2 H 2 , 2-15 N 1 ]glycine giving a mixture of compounds resulting from deuterium scrambling.
📜 SIMILAR VOLUMES
A synthetic route to stable-isotope-substituted L-phenyl-synthesized from both aromatic precursors by initial conversion into sodium phenylpyruvate and subsequent alanine is presented, which allows the introduction of 13 C, 15 N, and deuterium labels at any position or combination of transformation
## Abstract We have developed methods for the preparation of L‐glutamic acid, isotopically labeled with ^13^C, using commercially available purified enzymes. The procedure is sufficiently versatile that L‐glutamic acid may be labeled at any carbons or any combination of carbons using ^13^C‐labeled
## Abstract ChemInform is a weekly Abstracting Service, delivering concise information at a glance that was extracted from about 100 leading journals. To access a ChemInform Abstract of an article which was published elsewhere, please select a “Full Text” option. The original article is trackable v
The synthesis of the ' 4C labelled peptide glycyl-L-proly1-L- ## leucyl-' C ( U ) ] glycyl-L-proline (I) with the specific activity of 50 pCi/mMole was performed by the Merrifield solid phase method. The peptide (I) was degraded by Achromobacter iophagus collagenase.