Exchange rates and numbers of annular lipids for the calcium and magnesium ion dependent adenosinetriphosphatase.
A spin-labeled phospholipid is used to study lipid-protein interactions in the (Ca2+,Mg2+)-ATPase of sarcoplasmic reticulum from muscle. A novel null method is used to decompose composite electron spin resonance spectra into two components, characteristic of immobilized and mobile environments. Calculations based on a random mixing model suggest that protein-protein interactions will be relatively rare in these systems and that the immobilized lipid does not represent lipid trapped between proteins but rather represents annular phospholipid at the lipid-protein interface of the adenosinetriphosphatase. The apparent decrease in the amount of immobilized lipid with increasing temperature is shown to be consistent with lipid exchange between bulk and annulus, characterized by an exchange time of 10(-7) s at 37 degrees C. A minimum number of annular phospholipid sites of 32 and 22 are calculated at 0 and 37 degrees C, respectively.
East
J M
JM
Melville
D
D
Lee
A G
AG
D000818:Animals; D017301:Ca(2+) Mg(2+)-ATPase; D000252:Calcium-Transporting ATPases / Q000378:metabolism*; D004578:Electron Spin Resonance Spectroscopy; D007700:Kinetics; D008433:Mathematics; D010713:Phosphatidylcholines / Q000494:pharmacology; D010743:Phospholipids / Q000494:pharmacology*; D012519:Sarcoplasmic Reticulum / Q000201:enzymology; D013113:Spin Labels; D013816:Thermodynamics
D010713:Phosphatidylcholines; D010743:Phospholipids; D013113:Spin Labels; D017301:Ca(2+) Mg(2+)-ATPase; D000252:Calcium-Transporting ATPases; C017251:1,2-oleoylphosphatidylcholine