Leucylglycinamide released from oxytocin by human uterine enzyme

Roderich Walter; H. Shlank; J. D. Glass; I. L. Schwartz; T. D. Kerenyi

doi:10.1126/science.173.3999.827

Leucylglycinamide released from oxytocin by human uterine enzyme

Roderich Walter
, H. Shlank
, J. D. Glass
, I. L. Schwartz
, T. D. Kerenyi

Icahn School of Medicine at Mount Sinai

Research output: Contribution to journal › Article › peer-review

229 Scopus citations

Abstract

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 lencylglycinamide with the degradation of neurohypophyseal hormones.

Original language	English
Pages (from-to)	827-829
Number of pages	3
Journal	Science
Volume	173
Issue number	3999
DOIs	https://doi.org/10.1126/science.173.3999.827
State	Published - 1971

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title = "Leucylglycinamide released from oxytocin by human uterine enzyme",

abstract = "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 lencylglycinamide with the degradation of neurohypophyseal hormones.",

author = "Roderich Walter and H. Shlank and Glass, \{J. D.\} and Schwartz, \{I. L.\} and Kerenyi, \{T. D.\}",

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AU - Walter, Roderich

AU - Shlank, H.

AU - Glass, J. D.

AU - Schwartz, I. L.

AU - Kerenyi, T. D.

PY - 1971

Y1 - 1971

N2 - 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 lencylglycinamide with the degradation of neurohypophyseal hormones.

AB - 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 lencylglycinamide with the degradation of neurohypophyseal hormones.

UR - https://www.scopus.com/pages/publications/0015242348

U2 - 10.1126/science.173.3999.827

DO - 10.1126/science.173.3999.827

M3 - Article

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VL - 173

SP - 827

EP - 829

JO - Science

JF - Science

IS - 3999

ER -

Leucylglycinamide released from oxytocin by human uterine enzyme

Abstract

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