A novel method for the purification of 15-hydroxy-prostaglandin-dehydrogenase from swine lungs

15-Hydroxy-prostaglandin-dehydrogenase was purified 3 to 5 fold and with almost 100% yield from swine lungs by a novel method of precipitation with Rivanol after which it was further purified (8-10 fold) by gel-filtration. The optimal stability parameters of the purified enzyme preparation were determined and the behaviour of PGDH in polyacrylamide-gel-electrophoresis was studied by local enzyme detection. The enzyme seems to be composed of subunits. KM values of PGDH with respect to NAD, PGE2 and PGF2alpha were found to be 0.27, 0.017 and 0.038 mM, respectively.