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
收藏
页码：7 / 10
页数：4
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