从大鼠的趾长伸肌（EDL）和比目鱼肌中纯化肌钙蛋白C亚型。
Purification of troponin C isoforms from EDL and soleus muscles of the rat.
作者信息
O'Connell Brett, Stephenson Gabriela M M
机构信息
School of Biomedical Sciences, Victoria University of Technology, P.O. Box 14428, MCMC, Melbourne, Victoria 8001, Australia.
出版信息
J Muscle Res Cell Motil. 2003;24(8):555-9. doi: 10.1023/b:jure.0000009896.78385.16.
To date, there has been no report of rat TnC purification, despite the rat being an animal commonly used in physiological studies of mammalian muscle. In this study we isolated the fast and slow Troponin C isoforms from rat extensor digitorum longus (23 microg TnC/g wet weight) and soleus (17.6 microg TnC/g wet weight) muscles respectively. The rat Troponin C isoforms were shown to have identical electrophoretic properties to, and yield the same tryptic digestion products as commercial preparations of rabbit fast skeletal muscle and human cardiac muscle TnC isoforms.
尽管大鼠是哺乳动物肌肉生理学研究中常用的动物，但迄今为止，尚无大鼠肌钙蛋白C纯化的报道。在本研究中，我们分别从大鼠趾长伸肌（23微克肌钙蛋白C/克湿重）和比目鱼肌（17.6微克肌钙蛋白C/克湿重）中分离出快肌和慢肌肌钙蛋白C亚型。结果表明，大鼠肌钙蛋白C亚型与兔快肌骨骼肌和人心肌肌钙蛋白C亚型的商业制剂具有相同的电泳特性，并且产生相同的胰蛋白酶消化产物。
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