The effect of bilayer thickness and n-alkanes on the activity of the (Ca2+ + Mg2+)-dependent ATPase of sarcoplasmic reticulum.
The effect of bilayer thickness and n-alkanes on the activity of the (Ca2+ + Mg2+)-dependent ATPase of sarcoplasmic reticulum.
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DOI:
10.1016/s0021-9258(19)69855-8
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发表时间:
1981-02
期刊:
影响因子:
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通讯作者:
A. Johannsson;C. Keightley;G. Smith;C. D. Richards;T. Hesketh;J. Metcalfe
中科院分区:
文献类型:
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作者:
A. Johannsson;C. Keightley;G. Smith;C. D. Richards;T. Hesketh;J. Metcalfe
The activities of the (Ca2++ Mg2+)-ATPase from sar-coplasmic reticulum supported by a series of phosphatidylcholines (PC) with unsaturated (cis 9) fatty acyl chains (di (n: l) PC) varying in length from n= 12 to n= 23 were determined by the lipid titration technique (Warren, GB, Toon, P. A., Birdsall, N. J. M., Lee, A. G., and Metcalfe, J. C.(1974) Biochemistry 13, 5501-5507). The ATPase activity at 37 C increased with lipid chain length in the PC bilayer from 0.06 pmol min" mg" of protein (n= 12) to a maximum of 16 (n= 20) and decreased to 12 for complexes of the ATPase with di (23: l) PC. All ATPase activity changes with PC chain length were reversible by lipid exchange titrations. Bilayers containing mixtures of two di (n: l) PCs supported ATPase activities which corresponded approximately to the average chain length of the lipid mixture. The data indicate that the major factor determining ATPase activity in these complexes is the thickness of the lipid bilayer. The di (n: l) PC-ATPase complexes were treated with decane, previously shown to increase bilayer thickness in black lipid membranes of egg PC (Fettiplace, R., Andrews, D. M., and Haydon, D. A.