Abstract
THE ability of human pregnancy sera to inactivate oxytocin was first discovered by Fekete1 in 1930. The enzymatic nature of the reaction was later demonstrated by Werle et al.2,3. Using a biological method (the residual oxytocin after incubation with pregnancy serum being assayed on isolated rat's uterus) Werle and Semm4 demonstrated that a substantial part of the oxytocinase activity of the serum is recovered in the supernatant after half-saturation with ammonium sulphate. Moreover, using continuous electrophoresis, they localized the enzyme to the cathode side of the albumin flow.
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References
Fekete, K., Endokrinol., 7, 364 (1930).
Werle, E., and Effkemann, G., Arch. Gynaek., 171, 286 (1941).
Werle, E., Hevelke, A., and Buthmann, K., Biochem. Z., 309, 270 (1941).
Werle, E., and Semm, K., Arch. Gynaek., 187, 449 (1956).
Tuppy, H., and Nesvadba, H., Monatsch. Chem., 88, 977 (1957).
Tuppy, H., in Polypeptides which Affect Smooth Muscle and Blood Vessels (Pergamon Press, London, 1960).
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RIAD, A., SCANDRETT, F. Distribution of Cystine Aminopeptidase Activity (Oxytocinase) in Human Pregnancy Sera. Nature 193, 372–373 (1962). https://doi.org/10.1038/193372a0
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DOI: https://doi.org/10.1038/193372a0
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