Leucylglycinamide Released from Oxytocin by Human Uterine Enzyme

• Roderich Walter

  Departments of Physiology and Obstetrics and Gynecology, Mount Sinai Medical and Graduate Schools, City University of New York, New York 10029

• H. Shlank

  Departments of Physiology and Obstetrics and Gynecology, Mount Sinai Medical and Graduate Schools, City University of New York, New York 10029

• J. D. Glass

  Departments of Physiology and Obstetrics and Gynecology, Mount Sinai Medical and Graduate Schools, City University of New York, New York 10029

• I. L. Schwartz

  Departments of Physiology and Obstetrics and Gynecology, Mount Sinai Medical and Graduate Schools, City University of New York, New York 10029

• T. D. Kerenyi

  Departments of Physiology and Obstetrics and Gynecology, Mount Sinai Medical and Graduate Schools, City University of New York, New York 10029

抄録

Uteri of pregnant and nonpregnant women contain enzymic activities which inactivate oxytocin. A potent enzyme, which has been partially purified from uterine homogenates, cleaves the prolyl-leucyl peptide bond of oxytocin. This finding associates for the first time the release of the dipeptide leucylglycinamide with the degradation of neurohypophyseal hormones.

収録刊行物

• Science

  Science 173 (3999), 827-829, 1971-08-27

  American Association for the Advancement of Science (AAAS)

キーワード

• Multidisciplinary

詳細情報

• CRID: 1361137044772569472
• NII論文ID: 30020500512
• DOI: 10.1126/science.173.3999.827
• ISSN: 10959203
• ISSN: 00368075
• ISSN: http://id.crossref.org/issn/00368075
• Web Site: https://www.science.org/doi/pdf/10.1126/science.173.3999.827
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  • CiNii Articles