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The primary prostaglandin-inactivating enzyme of human placenta is a dimeric short-chain dehydrogenase

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Bioscience Reports

Abstract

The native form of NAD-dependent 15-hydroxyprostaglandin dehydrogenase of human placenta has a mol. wt. of about 50 0002 while the subunit tool. wt. is around 2g 0002 suggesting a dimeric quaternary structure. These propertie% the amino acid composition, insensitivity to EDTA, and inhibition patterns show general similarities to other short-chain dehydrogenases. Several hormones tested did not influence the activity of 15-hydroxyprostaglandin dehydrogenase2 but an unusual activation by two anti-depressant drugs was found and may relate to the existence of a natural regulatory factor.

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Authors and Affiliations

  1. Department of Biochemistry, University of Aberdeen, Marischal College, AB9 1AS, Aberdeen, Scotland, U.K.

    Oi Tong Mak & Jonathan Jeffery

  2. Department of Chemistry I, Karolinska Institutet, S-104 01, Stockholm 60, Sweden

    Hans Jörnvall

Authors
  1. Oi Tong Mak
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  2. Hans Jörnvall
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  3. Jonathan Jeffery
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Mak, O.T., Jörnvall, H. & Jeffery, J. The primary prostaglandin-inactivating enzyme of human placenta is a dimeric short-chain dehydrogenase. Biosci Rep 2, 503–508 (1982). https://doi.org/10.1007/BF01115248

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  • DOI: https://doi.org/10.1007/BF01115248

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