Purification and partial characterization of prostaglandin D2 11-keto reductase in rabbit liver

Biochim Biophys Acta. 1981 May 14;659(1):169-78. doi: 10.1016/0005-2744(81)90281-3.

Abstract

The cytoplasmic NADPH-dependent prostaglandin D2 11-keto reductase from rabbit liver was purified by a series of chromatographic procedures including isoelectric focusing. The enzyme catalyzed the conversion of prostaglandin D2 to prostaglandin F2 alpha and had a pH optimum of 7.0-7.5, and an isoelectric point of 5.8. The molecular weight was estimated to be 66 000 by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Enzymic activity was time and concentration dependent and required NADPH as cofactor.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Animals
  • Chromatography, DEAE-Cellulose
  • Hydroxyprostaglandin Dehydrogenases / isolation & purification*
  • Isoelectric Focusing
  • Liver / enzymology*
  • Male
  • NADP / metabolism
  • Platelet Aggregation / drug effects
  • Prostaglandins D / metabolism
  • Prostaglandins F / metabolism
  • Rabbits

Substances

  • Prostaglandins D
  • Prostaglandins F
  • NADP
  • Hydroxyprostaglandin Dehydrogenases
  • prostaglandin-F synthase