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热处理肌球蛋白丝的原子力显微镜观察

Atomic force microscopy of thermally treated myosin filaments.

作者信息

Iwasaki Tomohito, Washio Masahiro, Yamamoto Katsuhiro

机构信息

Department of Food Science, Rakuno Gakuen University, Ebetsu, Hokkaido 069-8501, Japan.

出版信息

J Agric Food Chem. 2005 Jun 1;53(11):4589-92. doi: 10.1021/jf0500381.

Abstract

Heat-induced morphological change in myosin filaments was observed using atomic force microscope. The thickness of fixed native myosin filament was estimated to be 95 +/- 5 nm. When myosin filaments in 0.1 M NaCl at pH 6.0 were heated at 40, 55, and 70 degrees C for 10 min, the particulate structure appeared spirally on the surface of the filament at 40 degrees C, and the thickness of the filament was 75 +/- 10 nm. When myosin filaments were treated at 55 degrees C, several filaments were formed associated with side-by-side interaction through projected myosin heads to form a strand. The surface of the strand looked knobby. The thickness of thermally denatured filaments at 55 degrees C was 48 +/- 5 nm, and that of strands was about 80-110 nm, indicating the involvement of several filaments in a strand. The strands became to be rope-like at 70 degrees C, and the individual filaments in a strand were not distinguishable.

摘要

使用原子力显微镜观察了热诱导的肌球蛋白丝形态变化。固定的天然肌球蛋白丝厚度估计为95±5纳米。当pH值为6.0的0.1 M NaCl中的肌球蛋白丝在40、55和70℃加热10分钟时,在40℃时细丝表面出现螺旋状颗粒结构,细丝厚度为75±10纳米。当肌球蛋白丝在55℃处理时,几条细丝通过突出的肌球蛋白头部并排相互作用形成一股。股线表面看起来有节。55℃时热变性细丝的厚度为48±5纳米,股线厚度约为80 - 110纳米,表明一股中涉及几条细丝。在70℃时股线变成绳状,一股中的单根细丝无法区分。

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