Abstract
Uridinediphospho-[U-14C]-D-galacturonic acid (UDP-[U-14C]-galacturonic acid) can be produced using UDP-D-glucuronic acid-4′-epimerase in radish root or mung bean hypocotyl enzyme particulate fractions. Epimerase activity was stable for several months at –70°C. Mung bean extracts had the highest activity per ng of protein. Enzymatic modification of UDP-[U-14C]-galacturonic acid and formation of 14C-breakdown products was reduced by short incubation times (<5 min). Using high performance liquid chromatography on an aminopropyl column, UDP-[U-14C]-galacturonic acid can be separated and collected without contamination by other products for use as a radiolabelled substrate for assay of galacturonan synthase with a yield of 14%.
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