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Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1972 Mar;69(3):533–534. doi: 10.1073/pnas.69.3.533

Human Placental 15-Hydroxyprostaglandin Dehydrogenase

Joseph Jarabak 1
PMCID: PMC426500  PMID: 4501572

Abstract

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 its Km 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.

Keywords: glycerol stabilization, pyridine nucleotide-linked enzyme, enzyme kinetics

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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