虾夷扇贝横纹肌和平滑肌的蛋白分布及理化性质

为探讨虾夷扇贝闭壳肌中横纹肌(ST)和平滑肌(SM)蛋白分布特征及理化性质差异。对肌肉组织进行切片、苏木精—伊红染色后,在光学显微镜下观察肌肉组织形态,SDS-PAGE分析蛋白组成,通过盐溶性和Ca~(2+)-ATPase对理化性质进行了比较研究。研究表明,横纹闭壳肌的肌纤维更粗,肌细胞间更致密;Myorod蛋白仅存在于平滑闭壳肌中,在横纹闭壳肌中不存在;副肌球蛋白在平滑闭壳肌中含量为31%,横纹肌中仅为11%。2种肌肉盐溶曲线也完全不同,在0.05~1.0 mol/L盐浓度范围内平滑肌的溶解性呈S型曲线上升,而横纹肌呈直线型上升,这种差异可能与副肌球蛋白含量有关。此外,平滑肌和横纹肌肌原纤维蛋白Ca~(2+)-ATPase最适温度分别为35和30°C,活化能分别为23.4和11.3 k J/mo L。

Protein distribution and physicochemical properties in striated muscle and smooth muscle of Patinopecten yessoensis

To explore the protein distribution and physicochemical properties differences between striated(ST)and smooth(SM) muscle of Patinopecten yessoensis, muscle tissue sections were stained with hematoxylin and eosin and observed under microscope.Protein composition was analyzed by SDS-PAGE.The physicochemical properties were compared by salt-soluble and Ca2+-ATPase.It was found that the striated muscle fibers were thicker and denser than smooth muscle .Myorod only existed in the smooth muscle and was not present in the striated muscle.The content of paramyosin in the smooth muscle was 31%, however, it was only 11% in striated muscle.There was a complete difference between the two kinds of salt solution curves.The smooth muscle solubility was characterized by S-shaped curve, which was different from the striated muscle and showed a linear rise in the range of 0.05–1.0 mol/L salt concentration.Such differences were probably caused by paramyosin content.In addition, the optimal temperature of Ca2+-ATPase in smooth muscle myofibrillar and striated muscle myofibrillar was 35 °C and 30 °C, and the activation energy was 23.4 kJ/moL and 11.3 kJ/moL, respectively.