Properties of prostacyclin synthase

Advances in Experimental Medicine and Biology
Volker UllrichI Siegle

Abstract

Prostacyclin synthase (PGIS) was isolated from bovine aortic microsomes after detergent solubilisation following purification by DEAE-Sephacel, immobilized metal affinity, and hydroxy apatite chromatography. The homogenous protein exhibited spectral characteristics of a heme-thiolate protein (P450) like the enzyme purified earlier from porcine microsomes and had an apparent mass of 52 kDa on SDS/PAGE. Three peptides from an endoproteinase Lys-C digest were isolated and sequenced. An antiserum was prepared from rabbits and purified by affinity chromatography. This allowed Western blots of microsomes from cultured endothelial cells. After treatment with IL-1 the activity of the cells in producing 6-keto-PGF1 alpha increased about threefold over 27 h which was accompanied by an increase in PGIS mass. A monoclonal antibody was used to set up an ELISA which served for the quantitation of PGIS in bovine tissues.

Citations

Nov 8, 2016·Drug Metabolism Reviews·Ahmed A El-Sherbeni, Ayman O S El-Kadi
Jul 5, 2003·Placenta·J A KeelanM D Mitchell
Apr 15, 2004·Biochemical and Biophysical Research Communications·A DaiberV Ullrich

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