Thermodynamics of the interaction between oxytocin and its myometrial receptor in sheep: a stepwise binding mechanism

Result code in IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60461373%3A22330%2F14%3A43897717" target="_blank" >RIV/60461373:22330/14:43897717 - isvavai.cz</a>

Result on the web

<a href="http://dx.doi.org/10.1016/j.bcp.2014.06.025" target="_blank" >http://dx.doi.org/10.1016/j.bcp.2014.06.025</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1016/j.bcp.2014.06.025" target="_blank" >10.1016/j.bcp.2014.06.025</a>

Result language

angličtina

Original language name

Thermodynamics of the interaction between oxytocin and its myometrial receptor in sheep: a stepwise binding mechanism

Original language description

Entropy (deltaS), enthalpy (deltaH) and heat capacity (deltaCp) changes attending the oxytocin interaction with its two binding sites on myometrial cell membranes in sheep were derived from the temperature dependence of Kd values. The high affinity oxytocin site (Kd on the order of 10?9 mol l?1, 25 °C), ascribed to the oxytocin receptor (OXTR), is entropy-driven in the temperature range 0-37 °C. Enthalpy component prevails as a driving force in the binding to the low affinity site (Kd ? 10?7) within thehigher temperature range. deltaCp values in both cases do not differ significantly from zero but become highly relevant in the presence of a GTP analog (10?4 M GTP-gamaS). Under these conditions, deltaCp in the low site interaction becomes negative anddeltaS is shifted toward negative values (enthalpy drift); deltaCp of the high affinity site rises to a high positive value and the interaction is even more strongly entropy driven. Atosiban, a competitive antagonist of oxytocin at OXTR d

Czech name

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Czech description

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Type

J_x - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)

CEP classification

CE - Biochemistry

OECD FORD branch

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Project

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Continuities

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Publication year

2014

Confidentiality

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Name of the periodical

Biochemical Pharmacology

ISSN

0006-2952

e-ISSN

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Volume of the periodical

91

Issue of the periodical within the volume

1

Country of publishing house

GB - UNITED KINGDOM

Number of pages

9

Pages from-to

119-127

UT code for WoS article

000340231300012

EID of the result in the Scopus database

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