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[转化甾体对钠钾ATP酶作用的分子极性依赖性]

[Molecular polarity dependence of the transformed steroid effect on Na,K-ATPase].

作者信息

Kamernitskiĭ A V, Reshetova I G, Mirsalikhova N M, Levi V G, Chernoburova E I

出版信息

Biokhimiia. 1984 Feb;49(2):316-20.

PMID:6324892
Abstract

The transformed steroids containing an additional cycle E (delta-lactone or 16.23-pyranone) or 23-carbethoxy side chain (1.10(-5) M) inhibit Na,K-ATPase from pig kidney medulla. The steroid structure has a noticeable effect on ATPase inhibiton varying from 9 to 35%. The data obtained suggest that the position, stereochemistry and the uneven distribution of polar substituents in the steroid molecule are essential for ATPase inhibition by steroid aglycons.

摘要

含有额外环E(δ-内酯或16,23-吡喃酮)或23-乙氧羰基侧链(1.10(-5)M)的转化甾体抑制猪肾髓质中的钠钾ATP酶。甾体结构对ATP酶抑制作用有显著影响,抑制率在9%至35%之间变化。所得数据表明,甾体分子中极性取代基的位置、立体化学和不均匀分布对于甾体苷元抑制ATP酶至关重要。

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