The use of the key enzyme involved in carbon-fluorine bond formation in Streptomyces cattleya catalysing the formation of 5'-fluoro-5'-deoxyadenosine (5'-FDA) from fluoride ion and S-adenosyl-L-methionine (SAM) was explored for its potential application in fluorine-18 labelling of the adenosine derivative. Enzymatic radiolabelling of [F-18]-5'-FDA was successfully carried out starting from SAM and [F-18]HF when the concentration of the enzyme preparation was increased from sub-mg/ml values to mg/ml values. The purity of the enzyme had no measurable effect on the radiochemical yield of the reaction and the radiochemical purity of [F-18]-5'-FDA. Copyright (C) 2003 John Wiley Sons, Ltd.
|Number of pages
|Journal of Labelled Compounds and Radiopharmaceuticals
|Published - Nov 2003
- enzymatic radiolabelling
- [F-18]-5 '-FDA