CARP NATURAL ACTOMYOSIN - THERMAL-DENATURATION MECHANISM
CARP NATURAL ACTOMYOSIN - THERMAL-DENATURATION MECHANISM
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DOI：
10.1111/j.1365-2621.1994.tb08177.x
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发表时间：
1994-09-01
影响因子：
3.9
通讯作者：
TSUCHIYA, T
中科院分区：
文献类型：
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作者：
SANO, T;OHNO, T;TSUCHIYA, T
肌球蛋白是肌肉的主要蛋白质，加热时其结构的变化已被ATP酶活性所估计。本研究采用生物物理和生物化学技术研究了鲤鱼肌动球蛋白分子在加热条件下的变化。肌动球蛋白分子在大约30摄氏度时开始展开。疏水性氨基酸残基和SH基团，原来在分子内部，出现到表面。由于疏水相互作用和二硫键，肌动球蛋白分子形成聚集体。在> 40 ℃时，部分肌球蛋白分子从肌动蛋白丝上解离。因此，解离的肌球蛋白和缺乏肌球蛋白的分子共存。此外，还观察到肌动蛋白丝的断裂，这与肌球蛋白分子的解离有关。在大于或等于60 ℃时，肌动球蛋白分子形成较大的聚集体，其中未观察到丝状形状。这种聚集主要通过SS键的形成而发生。
Structural changes of actomyosin, the major protein of muscle, on heating have been estimated on ATPase activity. We investigated carp actomyosin molecule changes on heating based on biophysical and biochemical techniques. Actomyosin molecules began to unfold at approximate to 30 degrees C. Hydrophobic amino acid residues and SH groups, which had been inside the molecule, emerged to the surface. Because of hydrophobic interactions and disulfide bonds, actomyosin molecules formed aggregates. At > 40 degrees C, a part of myosin molecules was dissociated from actin filaments. Thus, dissociated myosin and the myosin-lacking molecules co-existed. In addition, fragmentation of actin filaments was observed, which was associated with the dissociation of myosin molecules. At greater than or equal to 60 degrees C actomyosin molecules formed larger aggregates, in which no filamentous shape was observed. This aggregation occurred mainly by formation of SS bonds.