%0 Journal Article
%T EFFECT OF PHOSPHATIDYLCHOLINES ON THE DYNAMIC MICROSTRUCTURE OF PHOSPHORYLATION DOMAIN OF Ca~(2-)-ATPase FROM RABBIT SARCOPLASMIC RETICULUM<br>磷脂酰胆碱对兔骨骼肌肌质网钙泵磷酸化微区分子运动的影响
%A 朱明晏
%A 宋力群
%A 小山富康
%J 生物物理学报
%D 1993
%I 
%X With a nanosecond time -resolved fluorometer. the effect of phospholipids on the intramolecular dynamic microstructure of Ca2+-ATPase form rabbit sarcoplasmic reticulum was studied. Ca2+-ATPase was purified and reconstituted into vesicles and phospholipids surrounding the hydrophobic segment of Ca26-ATPase were exchanged with phosphatidylcholines of longer acyl chain length by lipid titration. The results showed that the replacement could lead to a decrease in membrane viscosity and Ca2+-ATPase activity. The half-decay tune of ANM fluorescence anisotropy was 72 ± 4ns in the control vesicles. 67± 3ns in di(20:4)PC titration vesicles. Concomitantly. observed decreases in membrane viscosity and Ca2+-ATPase activity suggest that the decreased membrane viscosity destabilized the Ca2+ -ATPase protein structure causing a reduction in Ca2+-ATPase activity.
%K Ca2--ATPase Phosphorylation domain Dynamic microstructure Lipid titration Protein-lipid interaction<br>钙泵
%K 磷酸化微区
%K 磷脂酰胆碱
%U http://www.alljournals.cn/get_abstract_url.aspx?pcid=90BA3D13E7F3BC869AC96FB3DA594E3FE34FBF7B8BC0E591&jid=E0C9D9BBED813D6674AC13E942EAC86D&aid=31A05CF781B27B05B142397BF169F520&yid=D418FDC97F7C2EBA&vid=9CF7A0430CBB2DFD&iid=38B194292C032A66&sid=44FDB9366EDDFA2B&eid=A22854835F81B3F8&journal_id=1000-6737&journal_name=生物物理学报&referenced_num=0&reference_num=1