Methods for the enzymatic synthesis of tyrosine and phenylalanine labeled with nitrogen-13

Autor:	Yasuhisa Asano, Sabina Filc-DeRicco, Karen C. Rosenspire, Edward Nieves, Arthur J.L. Cooper, Alan S. Gelbard
Rok vydání:	1990
Předmět:	chemistry.chemical_classification Nitrogen Radioisotopes Phenylalanine hydroxylase biology Chemistry Stereochemistry Transamination Phenylalanine General Engineering Tryptophan Enzymes Immobilized Phenylalanine dehydrogenase Enzyme Isotope Labeling biology.protein Tyrosine Amination
Zdroj:	International journal of radiation applications and instrumentation. Part A, Applied radiation and isotopes. 41(2)
ISSN:	0883-2889
Popis:	L-[13N]Tyrosine and L-[13N]phenylalanine were synthesized using immobilized enzymes by two methods. In method 1, [13N]ammonia is converted to L-[13N]glutamate; transamination with p-hydroxyphenylpyruvate yields L-[13N]tyrosine. [13N]Tyrosine is separated from other labeled intermediates on a Poropak Q column. In method 2, phenylalanine dehydrogenase catalyzes the reversible reductive [13N]amination of either phenylpyruvate or p-hydroxyphenylpyruvate to form L-[13N]phenylalanine or L-[13N]tyrosine, respectively. The feasibility of labeling DOPA and tryptophan with 13N was also demonstrated.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d0220a98f551230fecbc43e9c101559e https://pubmed.ncbi.nlm.nih.gov/2158948 Zobrazit plný text záznamu