Strohsacker M W, Minnich M D, Clark M A, Shorr R G, Crooke S T
Department of Molecular Pharmacology, Smith Kline & French Laboratories, King of Prussia, PA 19406-0937.
J Chromatogr. 1988 Jan 1;435(1):185-92. doi: 10.1016/s0021-9673(01)82173-7.
The cardiac muscle proteins, myosin and actin, were purified in one step using a salicylate-silica affinity column. The affinity columns were prepared by coupling sodium salicylate via its hydroxyl group to an Altex Ultraffinity-EP column. Crude detergent extracts from guinea pig hearts were passed through the column and the myosin-actin complex was then eluted with excess free salicylate or high salt. The affinity of cardiac myosin for immobilized salicylate was unique as myosin heavy chain from guinea pig leg muscle detergent extracts could not be purified by this procedure. Commercially purified rabbit leg muscle myosin also appeared to have no interaction with the salicylate affinity column, suggesting that the column is specific for cardiac myosin.
利用水杨酸-硅胶亲和柱一步纯化心肌蛋白肌球蛋白和肌动蛋白。通过将水杨酸钠经其羟基偶联到Altex Ultraffinity-EP柱上来制备亲和柱。将豚鼠心脏的粗制去污剂提取物通过该柱，然后用过量的游离水杨酸或高盐洗脱肌球蛋白-肌动蛋白复合物。心肌肌球蛋白对固定化水杨酸的亲和力是独特的，因为豚鼠腿部肌肉去污剂提取物中的肌球蛋白重链不能通过此方法纯化。商业纯化的兔腿部肌肉肌球蛋白似乎也与水杨酸亲和柱没有相互作用，这表明该柱对心肌肌球蛋白具有特异性。
