Cross R A, Vandekerckhove J
FEBS Lett. 1986 May 12;200(2):355-60. doi: 10.1016/0014-5793(86)81168-1.
Chymotryptic digestion of chicken gizzard light meromyosin (LMM) produced a 72 kDa core fragment, which was fully soluble at 150 mM KCl, pH 6.5-7.5. The fragment showed weak self-association at 50 mM KCl. The homology of the N-terminus amino acid sequence of this fragment with the sequence of the rabbit skeletal myosin rod suggested that the N-terminus of the core fragment originated 5 kDa from the hinge common to both smooth and skeletal myosin rod. Sedimentation experiments indicated that the domain specifying the insolubility of the intact LMM was 13 kDa long. Progressive proteolytic shortening of this region produced LMM fragments of progressively increasing solubility. Electron microscopy of segments formed from full-length LMM and from LMM core suggested that this 13 kDa domain specified the 43 nm parallel and antiparallel molecular overlaps characteristic of self-assembled intact myosin.
用胰凝乳蛋白酶消化鸡砂囊轻酶解肌球蛋白（LMM）产生了一个72 kDa的核心片段，该片段在150 mM KCl、pH 6.5 - 7.5条件下完全可溶。该片段在50 mM KCl时表现出弱的自我缔合。此片段N端氨基酸序列与兔骨骼肌肌球蛋白杆序列的同源性表明，核心片段的N端起源于平滑肌和骨骼肌肌球蛋白杆共同的铰链处5 kDa处。沉降实验表明，决定完整LMM不溶性的结构域长13 kDa。该区域的逐步蛋白酶解缩短产生了溶解度逐渐增加的LMM片段。对全长LMM和LMM核心形成的片段进行电子显微镜观察表明，这个13 kDa的结构域决定了自组装完整肌球蛋白特有的43 nm平行和反平行分子重叠。
