兔骨骼肌肌膜的特性分析
Characterization of sarcolemma from rabbit skeletal muscle.
作者信息
Drabikowski W, Zubrzycka E
出版信息
Recent Adv Stud Cardiac Struct Metab. 1976;9:133-47.
Sodium dodecyl sulfate polyacrylamide gel electrophoresis reveals in the rabbit skeletal muscle sarcolemma the presence of four major protein bands corresponding to molecular weight 216,000, 110,000, 44,000, 15,000, and smaller amounts of 148,000, 78,000, 68,000, 37,000, 27,000 proteins. (Na+-K+)-ATPase isolated from rabbit skeletal muscle contains 102,000, 44,000, and 32,000 protein bands. Sarcolemma is resistant to the solubilizing effect of Triton X-100, Lubrol, and deoxycholate. Sarcolemmal proteins, especially sodium-potassium-ATPase, are sensitive to digestion with trypsin.
十二烷基硫酸钠聚丙烯酰胺凝胶电泳显示，兔骨骼肌肌膜存在四条主要蛋白带，分子量分别为216,000、110,000、44,000、15,000，还有少量分子量为148,000、78,000、68,000、37,000、27,000的蛋白。从兔骨骼肌分离出的（钠钾）-ATP酶含有分子量为102,000、44,000和32,000的蛋白带。肌膜对Triton X-100、Lubrol和脱氧胆酸盐的增溶作用具有抗性。肌膜蛋白，尤其是钠钾ATP酶，对胰蛋白酶消化敏感。
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