FEBS Letters | |
The mitochondrial ATP synthase inhibitor protein binds near the C‐terminus of the F1 β‐subunit | |
Jackson, Philip J.1  Harris, David A.1  | |
[1] Department of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, England | |
关键词: Mitochondria; ATP synthase; F1 -ATPase; ATPase inhibitor protein; (Bovine heart); EEDQ; N-ethoxycarbonyl-2-ethoxy-1; 2-dihydroquinoline; HPLC; high-performance liquid chromatography; IF1; mitochondrial ATP synthase inhibitor protein; PTH; phenylthiohydantoin; SDS-PAGE; SDS-polyacrylamide gel electrophoresis; | |
DOI : 10.1016/0014-5793(88)80832-9 | |
学科分类:生物化学/生物物理 | |
来源: John Wiley & Sons Ltd. | |
【 摘 要 】
The specific, mitochondrial ATP synthase protein (IF1) was covalently cross-linked to its binding site on the catalytic sector of the enzyme (F1-ATPase). The cross-linked complex was selectively cleaved, leaving IF1 intact to facilitate the subsequent purification of the F1 fragment to which IF1 was cross-linked. This fragment was identified by sequence analysis as comprising residues 394–459 on the F1 β-subunit, near the C-terminus. This finding is discussed in the light of secondary structure predictions for both IF1 and the F1 β-subunit, and sequence homologies between mitochondrial and other ATP synthases.
【 授权许可】
Unknown
【 预 览 】
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