Abstract
A tritium labelled phospholipase A2 (PLA2) amide analogue inhibitor was prepared by the reduction of an alkene precursor. Diimide, heterogeneous and homogeneous metal catalyzed reduction methods were assessed for their suitability for the preparation of a tritiated ligand for 3H NMR spectroscopic studies. The chosen homogeneous metal-catalyzed method gave a product of specific activity 57 Ci mmol−1, which was isolated by flash chromatography. The binding of this tritiated substrate to bovine pancreatic PLA2 was observed by 3H NMR spectroscopy in the presence of calcium ions. Chemical shift changes suggest that the tritium atoms are located within the hydrophobic pocket of the protein, close to two phenylalanine residues.
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