DePover A, Lee S W, Matlib M A, Whitmer K, Davis B A, Powell T, Schwartz A
Biochem Biophys Res Commun. 1983 May 31;113(1):185-91. doi: 10.1016/0006-291x(83)90449-7.
[3H]Nimodipine binding was studied in isolated myocytes from rat heart and in partially purified sarcolemma, sarcoplasmic reticulum and mitochondrial fractions from dog heart. In isolated myocytes, the density of [3H]nimodipine specific sites (10(6) per cell) was close to density of [3H]QNB sites (0.8 x 10(6) per cell) and higher than that of [3H]DHA sites (0.2 x 10(6) per cell). During subcellular fractionation, [3H]nimodipine binding did not copurify with plasma membrane markers. The highest densities were found in fractions enriched in sarcolemma or in sarcoplasmic reticulum. No specific binding was found in mitochondria. These results indicate that the localization of [3H]nimodipine sites is not restricted to areas of the plasma membrane rich in beta-adrenoceptors, muscarinic receptors and sodium pump sites.
研究了[3H]尼莫地平在大鼠心脏分离心肌细胞以及犬心脏部分纯化的肌膜、肌浆网和线粒体组分中的结合情况。在分离的心肌细胞中,[3H]尼莫地平特异性位点的密度(每细胞10(6)个)接近[3H]QNB位点的密度(每细胞0.8×10(6)个),且高于[3H]DHA位点的密度(每细胞0.2×10(6)个)。在亚细胞分级分离过程中,[3H]尼莫地平结合并未与质膜标记物共纯化。在富含肌膜或肌浆网的组分中发现了最高密度。在线粒体中未发现特异性结合。这些结果表明,[3H]尼莫地平位点的定位并不局限于富含β-肾上腺素能受体、毒蕈碱受体和钠泵位点的质膜区域。