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3,4,5-Triiodobenzoic acid affects [3H]verapamil binding to plant and animal membrane fractions and smooth muscle contraction.

作者信息

Andrejauskas E, Hertel R, Marmé D

出版信息

Biochem Biophys Res Commun. 1986 Aug 14;138(3):1269-75. doi: 10.1016/s0006-291x(86)80420-x.

DOI:10.1016/s0006-291x(86)80420-x
PMID:3753496
Abstract

3,4,5-Triiodobenzoic acid, known as auxin transport inhibitor, stimulates specific [3H]verapamil binding to zucchini microsomes by 100% (EC50 = 1 microM). This stimulatory effect is due to a decrease of the apparent equilibrium dissociation constant KD for verapamil from 60 nM to 33 nM without significantly changing the maximum number of binding sites. 3,4,5-Triiodobenzoic acid also increases specific [3H]verapamil binding to rabbit skeletal muscle membranes (EC50 greater than or equal to 20 microM) without affecting [3H]nitrendipine and [3H]-d-cis-diltiazem binding. If 3,4,5-triiodobenzoic acid is added to isolated rings of rabbit A. saphena contracted by potassium depolarization, a dose-dependent relaxation is observed with an IC50 value of about 8 microM. Contractions initiated by the addition of 3 microM norepinephrine can also be abolished by 3,4,5-triiodobenzoic acid with half maximal inhibition at 40 microM.

摘要

相似文献

1
3,4,5-Triiodobenzoic acid affects [3H]verapamil binding to plant and animal membrane fractions and smooth muscle contraction.
Biochem Biophys Res Commun. 1986 Aug 14;138(3):1269-75. doi: 10.1016/s0006-291x(86)80420-x.
2
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7
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Partial purification of a protein from maize (Zea mays) coleoptile membranes binding the Ca2+-channel antagonist verapamil.
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