The primary prostaglandin-inactivating enzyme of human placenta is a dimeric short-chain dehydrogenase
Open Access
- 1 July 1982
- journal article
- research article
- Published by Portland Press Ltd. in Bioscience Reports
- Vol. 2 (7) , 503-508
- https://doi.org/10.1007/bf01115248
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.This publication has 17 references indexed in Scilit:
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