title: Purification of the human placental NAD-linked 15-hydroxyprostaglandin dehydrogenase.
abstract: An NAD-linked 15-hydroxyprostaglandin dehydrogenase has been purified 13,100-fold from human placental tissue. The specific activity of the purified enzyme ranges from 6900 to 8300 mU/mg protein depending on the method used to determine the protein concentration. On discontinuous electrophoresis in sodium dodecyl sulfate more than 95% of the protein migrates as a single band; its estimated molecular weight is 25.5-26.0 kDa. This is half the value obtained when the molecular weight is estimated under non-denaturing conditions and suggests that the enzyme is composed of two identical or nearly identical subunits.
authors.affiliation: Department of Medicine, University of Chicago School of Medicine, IL 60637.
authors.forename: J
authors.initials: J
authors.lastname: Jarabak
authors.forename: J D
authors.initials: JD
authors.lastname: Watkins
mesh_terms: D004591:Electrophoresis, Polyacrylamide Gel; D006801:Humans; D006911:Hydroxyprostaglandin Dehydrogenases / Q000302:isolation & purification*; D008970:Molecular Weight; D009243:NAD / Q000378:metabolism; D010920:Placenta / Q000201:enzymology*
chemical_list: D009243:NAD; D006911:Hydroxyprostaglandin Dehydrogenases