Vikhliantsev I M, Podlubnaia Z A
Biofizika. 2004 May-Jun;49(3):430-5.
By the use of modified SDS electrophoresis in agarose-strengthened 2% polyacrylamide gels, the adaptive behavior of titin isoforms in skeletal and cardiac muscles of ground squirrels (Citellus undulatus) during hibernation was studied. The presence of two titin isoforms (short and long) with molecular weights approximately 3700 and approximately 3800 kDa in m. soleus, approximately 3400 and approximately 3600 kDa in m. psoas, approximately 3000 and approximately 3400 kDa in the left ventricle of myocardium was found. It was found that the content of the short titin isoform in the above muscles of hibernating and arousing ground squirrels is considerably lower than that of the long titin isoform. The preservation of the long titin isoform in skeletal and cardiac muscles of hibernating and arousing ground squirrels can be regarded as an evolutionarily determined adaptive mechanism favoring the survival of animal under extreme conditions without pathological consequences.
通过在琼脂糖增强的2%聚丙烯酰胺凝胶中使用改良的SDS电泳，研究了地松鼠（Citellus undulatus）冬眠期间骨骼肌和心肌中肌联蛋白异构体的适应性行为。在比目鱼肌中发现了两种肌联蛋白异构体（短型和长型），分子量分别约为3700 kDa和约3800 kDa；在腰大肌中分别约为3400 kDa和约3600 kDa；在心肌左心室中分别约为3000 kDa和约3400 kDa。研究发现，冬眠和苏醒的地松鼠上述肌肉中短肌联蛋白异构体的含量明显低于长肌联蛋白异构体。冬眠和苏醒的地松鼠骨骼肌和心肌中长肌联蛋白异构体的保留可被视为一种进化决定的适应性机制，有利于动物在极端条件下生存而无病理后果。
