Isolation and amino acid sequence of the 9.5 kDa protein of beef heart ubiquinol:cytochrome c reductase

FEBS Letters

Schägger, H.¹  Borchart, U.¹  Machleidt, W.¹  von Jagow, G.¹  Link, T.A.¹ 

[1] Institut für Physiologische Chemie und Physikalische Biochemie, Goethestr. 33, 8000 München 2, FRG

关键词: Ubiquinol:cytochrome c reductase Primary structure Hydropathy profile Structure prediction Membrane protein (Beef heart mitochondria);   

DOI  :  10.1016/0014-5793(86)80515-4

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The 9.5 kDa protein of beef heart ubiquinol:cytochrome c reductase was isolated by a series of chromatographic steps involving dissociation of the complex by urea and guanidine. A clear distinction between the 9.5 kDa protein and the 9.2 kDa protein described earlier [(1982) J. Biochem. 91, 2077-2085] by SDS-PAGE was only achieved when the electrophoresis was performed according to Schägger et al. [(1985) FEBS Lett. 190, 89-94; (1986) Methods Enzymol. 126, 22] because in this gel system the apparent molecular mass of the 9.5 kDa protein is shifted to 11 kDa. The amino acid sequence was determined by solid-phase Edman degradation of the whole protein up to amino acid residue 80 and of the proteolytic cleavage fragments. The protein consists of 81 amino acid residues; its M _r was calculated to be 9507. Structure predictions have been made from average and sided hydropathy profiles. The 9.5 kDa protein is either bound to the core proteins within a 9.5 kDa-core protein subcomplex or else it aggregates easily with the core proteins during the isolation procedure.

【 授权许可】

Unknown