The bovine lung 20S proteasome binding to reversible inhibitors: modulation by sodium ion

被引：0

作者：

Eleuteri, AM ^{[1
]}

Angeletti, M ^{[1
]}

机构：

[1] Univ Camerino, Postgrad Sch Clin Biochim, Dept Mol Cellular & Anim Biol, I-62032 Camerino, MC, Italy

来源：

FEBS LETTERS | 2003年 / 547卷 / 1-3期

关键词：

20S proteasome; inhibition; sodium; linkage; signaling;

D O I：

10.1016/S0014-5793(03)00660-4

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The effect of sodium ion on the inhibition exerted by Cbz-Leu-Leu-Leu-CHO on the chymotrypsin-like activity of the 20S proteasome isolated from bovine lung was investigated. The experimental data were analyzed using a standard linkage formalism. The calculated equilibrium affinity constants for the sodium ion binding to the free-enzyme and the inhibitor-bound enzyme are compatible to other well-characterized ion-involving heterotropic systems. The functional interdependence between the binding events played by the inhibitor and the sodium ion conforms to a heterotropic modulatory mechanism. (C) 2003 Federation of European Biochemical Societies. Published by Elsevier Science B.V. All rights reserved.

引用

页码：7 / 10

页数：4

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