Narahara H T, Green J D
Biochim Biophys Acta. 1983 Apr 21;730(1):71-5. doi: 10.1016/0005-2736(83)90318-8.
Muscle proteins were labeled by incubating isolated frog sartorius muscles with [3H]- or [14C]phenylalanine. Sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis of plasma membrane fractions revealed a major protein band with an apparent molecular weight of approx. 96,000. Radioactivity in this band showed a clearly delineated decrease, relative to other bands, when previously labeled muscles were induced to contract either by electrical stimulation or by increasing the influx of Ca2+ from the incubation medium. It is postulated that a Ca2+-activated neutral protease may account for this decrease in labeled membrane protein.
通过将分离的青蛙缝匠肌与[3H] - 或[14C]苯丙氨酸孵育来标记肌肉蛋白。对质膜部分进行十二烷基硫酸钠（SDS）-聚丙烯酰胺凝胶电泳，显示出一条主要蛋白带，其表观分子量约为96,000。当通过电刺激或增加来自孵育培养基的Ca2 +流入量诱导先前标记的肌肉收缩时，该条带中的放射性相对于其他条带明显下降。据推测，一种Ca2 +激活的中性蛋白酶可能是标记膜蛋白减少的原因。
