Leucylglycinamide Released from Oxytocin by Human Uterine Enzyme
Leucylglycinamide Released from Oxytocin by Human Uterine Enzyme
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DOI：
10.1126/science.173.3999.827
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发表时间：
1971-08
期刊：
影响因子：
56.9
通讯作者：
R. Walter;H. Shlank;John D. Glass;Irving L. Schwartz;T. Kerenyi
中科院分区：
文献类型：
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作者：
R. Walter;H. Shlank;John D. Glass;Irving L. Schwartz;T. Kerenyi
妊娠和非妊娠妇女的子宫内含有促催产素的酶活性。一种从子宫匀浆中部分纯化的强效酶，可切割催产素的脯氨酰-亮氨酰肽键。这一发现首次将二肽亮氨酰甘氨酰胺的释放与神经垂体激素的降解联系起来。
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 findinig associates for the first time the release of the dipeptide leucylglycinamide with the degradation of neurohypophyseal hormones.