The primary prostaglandin-inactivating enzyme of human placenta is a dimeric short-chain dehydrogenase
Keyword(s):
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.
1982 ◽
Vol 39
(1)
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pp. 80-91
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2003 ◽
Vol 53
(2)
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pp. 282-289
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1984 ◽
Vol 222
(1227)
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pp. 259-271
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2004 ◽
Vol 55
(3)
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pp. 781-781
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2009 ◽
Vol 42
(2)
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pp. 169-173
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