[Isolation and purification of a NAD(+)-dependent 15-hydroxyprostaglandin dehydrogenase from human placenta].
A NAD(+)-dependent 15-hydroxyprostaglandin dehydrogenase has been isolated and purified from human placenta. About 9300-fold enrichment was achieved with a yield of 9.3%. The specific activity of the purified enzyme was 6470 nmol/min.mg. 15-OH-PGDH showed a single band on PAGE and two bands on SDS-PAGE. The molecular weights were approximately 26 and 52 kd, respectively. The two bands were recognized by both polycloning and monocloning antibodies of the enzyme. It is suggested that the 15-OH-PGDH be composed of two identical subunits.
Yang
J
J
College of Pharmacy, University of Kentucky.
Gao
Z
Z
Tai
H H
HH
D004591:Electrophoresis, Polyacrylamide Gel / Q000379:methods; D005260:Female; D006801:Humans; D006911:Hydroxyprostaglandin Dehydrogenases / Q000737:chemistry / Q000302:isolation & purification*; D010920:Placenta / Q000737:chemistry*; D011247:Pregnancy
D006911:Hydroxyprostaglandin Dehydrogenases; C035859:15-hydroxyprostaglandin dehydrogenase