[Role of interprotein interactions in the regulation of the sarcoplasmic reticulum Ca-pump].
The data on the structural state of sarcoplasmic reticulum membranes in skeletal muscles of rabbit were obtained by EPR-spectroscopy, fluorescent analysis and flash-photolysis and discussed in the paper. Comparison of the functional state of Ca-pump and variations in hydrophobic volume and membrane microviscosity permits concluding that thermoinduced anomalies of the enzymic activity are due to changes in the phase state of lipids. It is shown that changes in the physiochemical state of lipids affect the interprotein interactions in the oligomeric Ca-pump structure. In this case ATP weakens the interaction between Ca-pump globules, while a decrease in the hydrophobic membrane volume intensifies it. An assumption is advanced that the modifying ATP effect on Ca-pump is based on an increase in the functional independence of Ca2+-ATPase monomers, and therefore it is under the control of the membrane lipid phase.
D000818:Animals; D002118:Calcium / Q000378:metabolism*; D000252:Calcium-Transporting ATPases / Q000378:metabolism*; D004578:Electron Spin Resonance Spectroscopy; D007473:Ion Channels / Q000378:metabolism*; D007700:Kinetics; D008565:Membrane Proteins / Q000378:metabolism*; D009132:Muscles / Q000378:metabolism*; D010782:Photolysis; D011817:Rabbits; D012519:Sarcoplasmic Reticulum / Q000378:metabolism*; D013816:Thermodynamics
D007473:Ion Channels; D008565:Membrane Proteins; D000252:Calcium-Transporting ATPases; D002118:Calcium
Rol' mezhbelkovykh vzaimodeĭstviĭ v reguliatsii Ca-nasosa sarkoplazmaticheskogo retikuluma.