Division for Food Industry Platform Technology, Korea Food Research Institute, Seongnam-si, Gyeonggi-do 463-746, Republic of Korea.
Meat Sci. 2011 Mar;87(3):219-22. doi: 10.1016/j.meatsci.2010.10.012. Epub 2010 Nov 12.
To observe the role of sarcoplasmic protein (SP) on myofibrillar protein (MP) denaturation under a hydrostatic pressure (HP), MP isolated from bovine muscle was treated with 300 MPa by increasing concentrations of SP (0, 0.8, 1.6, and 3.2 mg/ml) from bovine. SDS-PAGE patterns of soluble proteins in 0.1M NaCl (pH 7.4) indicated that a protein (about 100 kDa) from MP decreased with increasing concentrations of SP and that a 97 kDa protein from SP observed with 0.1 MPa was not observed with 300 MPa. SDS-PAGE patterns of soluble proteins in 0.6 M NaCl (pH 7.4) and Ca-ATPase activity showed that the denaturation of myosin heavy chain (MHC) was accelerated with increasing SP concentrations with the 300 MPa treatment. Thus, the addition of SP enhanced HP-induced denaturation of MHC and of a protein from MP of about 100 kDa.
为了观察肌浆蛋白 (SP) 在静水压力 (HP) 下对肌原纤维蛋白 (MP) 变性的作用，从牛肌肉中分离出 MP，用浓度逐渐增加的 SP（0、0.8、1.6 和 3.2mg/ml）处理 300MPa 的 MP。在 0.1M NaCl（pH7.4）中可溶蛋白的 SDS-PAGE 图谱表明，来自 MP 的一种蛋白（约 100kDa）随 SP 浓度的增加而减少，而在 0.1MPa 时观察到的来自 SP 的 97kDa 蛋白在 300MPa 时则观察不到。在 0.6M NaCl（pH7.4）中的 SDS-PAGE 图谱和 Ca-ATPase 活性表明，随着 300MPa 处理时 SP 浓度的增加，肌球蛋白重链 (MHC) 的变性加速。因此，SP 的添加增强了 HP 诱导的 MHC 和来自 MP 的约 100kDa 蛋白的变性。
