Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0027960 (mole)
 21,279 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

15-Hydroxyprostaglandin dehydrogenase was isolated from human term placenta up to a final purification of 380-fold. A spec. act. of 2000 mU/mg of protein was reached. The preparation was not homogeneous as judged by analytical disc electrophoresis. The enzyme could be stored in the presence of 50% glycerol and 10mM 2-mercaptoethanol without any loss of activity for at least one year. A distinct single protein band stained after discontinuous polyacrylamide gel electrophoresis was shown by enzymatic activity staining to correspond to 15-hydroxyprostaglandin dehydrogenase activity. Thus no evidence for the exitstence of isoenzymes was obtained. The protein in the final preparation steps showed neither alcohol dehydrogenase, NAD reductase, nor NADH oxidase activity, nor enzymatic conversion of prostaglandin or 15-oxoprostaglandin in the absence of NAD and NADH. No spontaneous reactions between NAD and prostaglandin or NADH and 15-oxoprostaglandin were detectable in the absence of the enzyme. Ethanol and glycerol slightly inhibited the reaction. Various buffers (Tris/HC1, potassium phosphate, HEPES, and triethanolamine) and salts (ammonium chloride, ammonium sulfate, potassium chloride, and sodium chloride) had different effects on the reaction rate. The pH profile of the reaction shows a plateau between pH 7.0 and 7.8 and a steep maximum at pH 9.5. A linear Arrhenius plot was obtained for the temperature dependence of the reaction from 20 to 37 degrees C. The molar activation enthalpy of the reaction was calculated to be 13.1 kcal/mole. The molecular weight of 15-hydroxyprostaglandin dehydrogenase was estimated to be 32000 -/+ 3000 by gel filtration on Sephadex G-150 in the presence of 10mM mercaptoethanol.
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PMID:[15-Hydroxyprostaglandin dehydrogenase from human placenta. 1. Isolation and characterization]. 24 91

The high activity of 15-hydroxyprostaglandin dehydrogenase (PGDH) which catalyzes the first step in prostaglandin metabolism has been demonstrated in the human placenta. To investigate the role of placental PGDH (p-PGDH) in the perinatal period, PGDH activity was measured in 167 placentas of gestational ages 37 to 41 weeks. The activity was expressed as n mole/min/non heme protein of 15-keto-PGE2 which was produced by incubation of PGE2 and placental homogenate supernatant. The following data were obtained. p-PGDH activity was significantly lower at the 40 weeks of gestation than at other weeks. There was no difference in placental PGDH activity between cesarean section and vaginal delivery, and between the periods before and after onset labor of cesarean section. p-PGDH activity in the PGs administered group was higher than that in the non PGs group. p-PGDH activity of a male fetus was higher than that of a female. This suggests that p-PGDH activity is under the control of hormones. No relationship was observed between p-PGDH activity and other perinatal factors such as toxemia of pregnancy, parity, Apgar score, birth weight, placental weight, blood loss, and duration of labor.
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PMID:[Study on PGDH activity in human term placenta--relationship between PGDH activities and perinatal factors]. 387 84