Purification of the carboxy‐atractylate binding protein from mitochondria
Purification of the carboxy‐atractylate binding protein from mitochondria
复制标题
从线粒体中纯化羧基白术酸结合蛋白
DOI：
10.1016/0014-5793(75)80127-x
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发表时间：
1975
期刊：
影响因子：
3.5
通讯作者：
Martin Klingenberg
中科院分区：
文献类型：
--
作者：
Paolo Riccio;H. Aquila;Martin Klingenberg
The discovery of a specific ADP, ATP transport through the inner mitochondrial membrane [l] suggested early the existence of a specific carrier catalyzing this transport. At a subsequent stage the carrier was defined by the binding of the substrates, ADP and ATP, or the highly specific inhibitors, atractylate (ATR), carboxy-atractylate (CAT) and bongkrekate (BKA), which are assumed also to bind specifically to the ADP, ATP carrier [2-51. For the isolation of the ADP, ATP carrier it appeared most promising to use for its identificat. ion the tagging of the protein with the high affinity ligand carboxyatractylate which is available in the “S-1abelled form. Moreover, ADP, ATP binding had been found to be very sensitive to relatively minor alterations of the mitochondrial membrane in contrast to binding of 35 S-CAT.At first the identification of the CAT-binding protein by 3sS-CAT binding was unsuccessful because no specific binding of CAT was found after solubilization of the membranes with a variety of detergents. As reported a year ago [6] a breakthrough was achieved by loading the carrier in the parent mitochondria with CAT before extraction. By this means it was possible in particular with Triton X-100 to solubilize the CAT-protein complex and to apply standard fractionation procedures as reported in a following letter [7]. These communications should be read in context with the earlier report [6] on our
