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解离-重组实验支持线粒体F1中存在两个催化性β亚基。

Dissociation-reconstitution experiments support the presence of two catalytic beta-subunits in mitochondrial F1.

作者信息

Nieboer P, Hartog A F, Berden J A

机构信息

Laboratory of Biochemistry, University of Amsterdam, The Netherlands.

出版信息

Biochim Biophys Acta. 1987 Nov 19;894(2):277-83. doi: 10.1016/0005-2728(87)90197-6.

DOI:10.1016/0005-2728(87)90197-6
PMID:2890378
Abstract

Mitochondrial F1, inactivated to various extents with 4-chloro-7-nitrobenzo-2-oxa-1,3-diazole (NBD-Cl), was dissociated with LiCl and reconstituted after removal of the salt. This procedure resulted in a reactivation that corresponded with a reactivation theoretically expected on the basis of the assumption that the reassociation of beta-subunits into native F1 molecules is random and that two out of the three beta-subunits are directly involved in catalysis. Repeated inactivation of such reactivated F1, followed by the same dissociation-association procedure, resulted in similar data. After inactivation of F1 by covalent binding of 2-N-AT(D)P to one catalytic site, no reactivation upon dissociation-reassociation was obtained due to the fact that such modified F1 did not dissociate under the experimental conditions used.

摘要

用4-氯-7-硝基苯并-2-恶唑-1,3-二氮杂茂(NBD-Cl)在不同程度上使其失活的线粒体F1,用LiCl解离并在除去盐后进行重组。该程序导致了再活化,这与基于β亚基重新缔合成天然F1分子是随机的以及三个β亚基中有两个直接参与催化的假设理论上预期的再活化相对应。对这种再活化的F1进行重复失活,然后进行相同的解离-缔合程序,得到了相似的数据。在用2-N-AT(D)P共价结合到一个催化位点使F1失活后,由于这种修饰的F1在所用实验条件下不解离,因此解离-重组后未获得再活化。

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Bistability and control for ATP synthase and adenylate cyclase is obtained by the removal of substrate inhibition.通过消除底物抑制作用可实现ATP合酶和腺苷酸环化酶的双稳性及控制。
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