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牛心线粒体寡霉素敏感性赋予蛋白(OSCP)的氨基酸序列及其与大肠杆菌F1 - ATP酶δ亚基的同源性。

Amino acid sequence of the oligomycin sensitivity-conferring protein (OSCP) of beef-heart mitochondria and its homology with the delta-subunit of the F1-ATPase of Escherichia coli.

作者信息

Ovchinnikov Y A, Modyanov N N, Grinkevich V A, Aldanova N A, Trubetskaya O E, Nazimov I V, Hundal T, Ernster L

出版信息

FEBS Lett. 1984 Jan 23;166(1):19-22. doi: 10.1016/0014-5793(84)80036-8.

Abstract

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 delta-subunit of E. coli F1, based on the terminal amino acid sequences of OSCP, is further substantiated.

摘要

已报道了牛心线粒体中赋予寡霉素敏感性的蛋白质(OSCP)的完整氨基酸序列。该蛋白质含有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端1 - 77和C端128 - 190)中富含带电荷的氨基酸,而其中心区域则更具疏水性。基于OSCP的末端氨基酸序列,该蛋白质与大肠杆菌F1的δ亚基早期报道的同源性得到了进一步证实。

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