Biomedical subjects
J Jarabak
Publications and source records attributed to J Jarabak.
Human placental 15-hydroxyprostaglandin dehydrogenase.
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 K(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.
Studies on the soluble 17 -hydroxysteroid dehydrogenase from human placenta. Evidence for a subunit structure.
Explore the source record for details and available documents.
A soluble dihydrofolate reductase from human placenta: purification and properties.
Explore the source record for details and available documents.
The inhibition of the soluble human placental 17-beta-hydroxysteroid dehydrogenase by o,p -DDD and its analogs.
Explore the source record for details and available documents.
A souble 17 beta-hydroxysteroid dehydrogenase from human placenta. The binding of pyridine nucleotides and steroids.
Explore the source record for details and available documents.