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Total synthesis of fully tritiated leu‐enkephalin by enzymatic coupling
Author(s) -
Hellio F.,
Lecocq G.,
Morgat J. L.,
Gueguen P.
Publication year - 1990
Publication title -
journal of labelled compounds and radiopharmaceuticals
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.432
H-Index - 47
eISSN - 1099-1344
pISSN - 0362-4803
DOI - 10.1002/jlcr.2580280902
Subject(s) - chemistry , enkephalin , enzyme , residue (chemistry) , specific activity , tritium , carboxypeptidase , stereochemistry , receptor , chromatography , radiochemistry , biochemistry , opioid , physics , nuclear physics
This paper describes the total enzymatic synthesis of Leu‐enkephalin (Tyr‐Gly‐Gly‐Phe‐Leu) in which all residues were labelled with tritium. Carboxypeptidase Y from Saccharomyces cerevisiae was the coupling enzyme. [ 3 H]‐Tyr‐NH 2 , [ 3 H]‐Gly‐Oet, [ 3 H]‐Phe‐NH 2 and [ 3 H]‐Leu‐NH 2 were prepared with specific radioactivities ranging between 20 and 60 Ci/mmol (740 to 2220 GBq/mmol). Using a microscale procedure, we obtained a fully tritiated hormone having a specific radioactivity equal to 139 Ci/mmol (5143 GBq/mmol), in agreement with the summation of the specific radioactivities of constituting residue. The radioactive hormone had antigenic properties identical to those of native Leu‐enkephalin. It also bound to rat brain opiate receptors like the parental hormone.