Open AccessHuman Placental 15-Hydroxyprostaglandin Dehydrogenase
Author(s) -
Joseph Jarabak
Publication year - 1972
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.69.3.533
Subject(s) - dehydrogenase , enzyme , nad+ kinase , chemistry , biochemistry , glycerol , human placenta , placenta , biology , fetus , pregnancy , genetics
Normal, term, human placentas are a rich source of a 15-hydroxyprostaglandin dehydrogenase. The enzyme is extremely labile, and partial purification could be achieved only after stabilization with glycerol. The instability of the enzyme and itsK m for NAD are indications that it is different from the 15-hydroxyprostaglandin dehydrogenase isolated from swine lung. Human placental tissue should provide a very useful source from which large amounts of highly purified 15-hydroxyprostaglandin dehydrogenase may be obtained.