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首页> 外文期刊>FEBS Letters >Amino acid sequence of the oligomycin sensitivity‐conferring protein (OSCP) of beef‐heart mitochondria and its homology with the δ‐subunit of the F1‐ATPase of Escherichia coli
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Amino acid sequence of the oligomycin sensitivity‐conferring protein (OSCP) of beef‐heart mitochondria and its homology with the δ‐subunit of the F1‐ATPase of Escherichia coli

机译:牛肉心线粒体寡聚敏感性赋予蛋白(OSCP)的氨基酸序列及其与大肠杆菌F1-ATPaseδ亚基的同源性

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摘要

>The complete amino acid sequence of the oligomycin sensitivity-conferring protein (OSCP) of beef-heart mitochondria is reported. The protein contains 190 amino acids and has a molecular mass of 20 967. Its structure is characterized by a concentration of charged amino acids in the two terminal segments (N 1–77 and C 128–190) of the protein, whereas its central region is more hydrophobic. The earlier reported homology of the protein with the δ-subunit of E. coli F1, based on the terminal amino acid sequences of OSCP, is further substantiated.
机译:>报道了牛肉心线粒体赋予寡霉素敏感性的蛋白(OSCP)的完整氨基酸序列。该蛋白质包含190个氨基酸,分子量为20967。其结构的特征是在蛋白质的两个末端片段(N 1–77和C 128–190)中带电氨基酸的浓度较高,而其中心区域更疏水。较早报道该蛋白质与 E的δ-亚基具有同源性。基于OSCP末端氨基酸序列的大肠埃希菌F 1 得到进一步证实。

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