PLACENTAL TRANSFER OF DRUGS.
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Biomedical subjects
Publications and source records attributed to C A VILLEE.
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1. Measurements of kinetic constants for a purified preparation of human-placenta oestradiol dehydrogenase have been made. 2. These constants have been compared with similar measurements made on crude ammonium sulphate precipitates of human-placenta homogenates. The comparison indicates that nearly half of the observed nicotinamide nucleotide-transhydrogenation activity in the crude preparations is due to a specific oestrogen-dependent transhydrogenase. 3. The remainder of the observed activity results from a substrate-mediated transhydrogenation catalysed by the oestradiol-dehydrogenase activities present in the preparation.
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Sea urchin embryos grown in salt water containing L-malate showed a pattern of development of L-malate dehydrogenase which did not differ from that of embryos grown in s lt water. However, embryos grown in 10-(3)M D-malate for 6 or 12 hours had one additional band of L-malate dehydrogenase that was not present in control embryos of the same age.
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Sea urchin embryos at the 64-cell stage were dissociated by treatment with trypsin and separated by centrifugation on a sucrose gradient. The large blastomeres have two and the small blastomeres have three bands of L-malate dehydrogenase activity, which are separated by disk microelectrophoresis on polyacrylamide gel, whereas unfertilized eggs have five.
Injection of C(14)-labeled amino acids intraperitoneally into rat fetuses in utero results in greater labeling of fetal serum proteins than when the amino acid is injected into the mother. Maternal partial hepatectomy leads to only minimal changes in serum protein synthesis. Rat fetuses synthesize at least some of their serum proteins during the last 3 days of gestation.
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The nonparticulate fraction of homogenates of heart, liver, kidney, lung, and cerebral cortex from human fetuses of varying gestational ages was subjected to electrophoresis on starch grains. Five lactic dehydrogenases and two malic dehydrogenases with characteristic rates with pyridine nucleotide analogs were found in all tissues at all ages. Quantitative differences in the relative proportions of these peaks were observed as gestation proceeded.
Immunoelectrophoretic comparison of maternal and fetal rat serum proteins with antiserum to adult rat serum proteins showed a unique protein in the fetal serum. The fetal protein exhibited in agar gel electrophoresis a variable mobility that was dependent on concentration. The fetal protein reacted strongly with a nonspecific antiserum.
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