Leucylglycinamide released from oxytocin by human uterine enzyme.
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.
D002021:Buffers; D002247:Carbon Isotopes; D004586:Electrophoresis; D004798:Enzymes / Q000302:isolation & purification / Q000494:pharmacology*; D005260:Female; D005998:Glycine / Q000032:analysis / Q000378:metabolism; D006801:Humans; D007930:Leucine / Q000032:analysis / Q000378:metabolism; D010121:Oxytocin / Q000037:antagonists & inhibitors* / Q000378:metabolism; D011247:Pregnancy; D014020:Tissue Extracts / Q000494:pharmacology; D014599:Uterus / Q000201:enzymology*
D002021:Buffers; D002247:Carbon Isotopes; D004798:Enzymes; D014020:Tissue Extracts; D010121:Oxytocin; D007930:Leucine; D005998:Glycine