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- W2066565623 abstract "Plasma oxytocinase of pregnancy and three placental oxytocinase fractions from human placental extracts were compared. On the basis of acrylamide-agarose chromatography, polyacrylamide gel electrophoresis, substrate specificity, heat liability and relative insensitiveness to L-methionine, it is concluded that placental enzyme activities, present in the second acrylamide-agarose peak, are identical with the plasma pregnancy oxytocinase and are to be regarded as its source. The hypothesis of a transplacental passage of placental peak II oxytocinase in the blood compartment of the mother seems well supported. Heat treatment of the placental extracts uncovered a minor activity behaving like Oya's microsomal oxytocinase, which is totally unlike the plasma oxytocinase and plays no part in the increased oxytocinase activity of human pregnancy plasma. A hitherto undescribed enzyme activity shares with the pregnancy oxytocinase its specificity towards L-leucyl-beta-naphthylamide and di-S-S-L-cysteinyl-beta-naphthylamide, its heat lability and realtive insensitiveness to L-methionine. However, this activity is carried by a protein of much lower molecular weight as judged by acrylamide-agarose chromatography, which shows only a single activity band on polyacrylamide gel electrophoresis." @default.
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- W2066565623 date "1980-02-01" @default.
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- W2066565623 title "Human placental oxytocinase and its relationship to pregnancy plasma oxytocinase" @default.
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- W2066565623 doi "https://doi.org/10.1016/0009-8981(80)90062-5" @default.
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