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.
The primary prostaglandin-inactivating enzyme of human placenta is a dimeric short-chain dehydrogenase
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Oi Tong Mak, Hans Jörnvall, Jonathan Jeffery; The primary prostaglandin-inactivating enzyme of human placenta is a dimeric short-chain dehydrogenase. Biosci Rep 1 July 1982; 2 (7): 503–508. doi: https://doi.org/10.1007/BF01115248
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