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主动脉平滑肌肌球蛋白片段的蛋白酶敏感位点及特性

Protease-susceptible sites and properties of fragments of aortic smooth-muscle myosin.

作者信息

King L, Jiang M J, Huang T S, Sheu G C

机构信息

Department of Biochemistry, Chang Gung Medical College, Tao-Yuan, Republic of China.

出版信息

Biochem J. 1995 Dec 1;312 ( Pt 2)(Pt 2):511-8. doi: 10.1042/bj3120511.

DOI:10.1042/bj3120511
PMID:8526864
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC1136292/
Abstract

We have examined the protease susceptibility of aortic myosin, the thermal unfolding profiles of myosin rod and light meromyosin (LMM) and the solubility properties of the LMM fragments. Two major protease-susceptible sites were found, located at the head-rod junction and the heavy meromyosin (HMM)-LMM junction. Both tryptic and chymotryptic digestion of aortic myosin rod produced the LMM (80-85 kDa) and short subfragment 2 (S-2) (40-45 kDa) segments, which were similar to those of gizzard myosin rod and differed from the short LMM (70 kDa) and long S-2 (58 kDa) segments produced from skeletal-muscle rod. The thermal unfolding profile of aortic myosin rods exhibited three helix-unfolding transitions, at 47.5, 51 and 54 degrees C, similar to those of gizzard rods yet different from those of skeletal-muscle rods. There was a dramatic difference in the solubility of aortic LMM fragments of various molecular mass, as for gizzard smooth-muscle LMM and rabbit skeletal-muscle LMM. LMM fragments of molecular mass 77 kDa or more were completely insoluble in low-ionic-strength buffer, whereas LMM fragments of molecular mass 73 kDa or less were completely soluble in low-ionic-strength buffer. Proteolytic digestion patterns of LMM showed two additional protease-susceptible sites located 13 and 30 kDa from the ends of the LMM molecule. This suggests the existence of flexible regions within the LMM molecule, which may be responsible for the folded form of aortic myosin.

摘要

我们研究了主动脉肌球蛋白对蛋白酶的敏感性、肌球蛋白杆和轻酶解肌球蛋白（LMM）的热解折叠谱以及LMM片段的溶解性。发现了两个主要的蛋白酶敏感位点，分别位于头部-杆连接处和重酶解肌球蛋白（HMM）-LMM连接处。主动脉肌球蛋白杆经胰蛋白酶和糜蛋白酶消化均产生LMM（80 - 85 kDa）和短亚片段2（S-2，40 - 45 kDa）片段，这些片段与砂囊肌球蛋白杆的片段相似，与骨骼肌杆产生的短LMM（70 kDa）和长S-2（58 kDa）片段不同。主动脉肌球蛋白杆的热解折叠谱在47.5、51和54摄氏度呈现出三个螺旋解折叠转变，与砂囊肌球蛋白杆的相似，但与骨骼肌杆的不同。各种分子量的主动脉LMM片段的溶解性存在显著差异，砂囊平滑肌LMM和兔骨骼肌LMM也是如此。分子量77 kDa及以上的LMM片段在低离子强度缓冲液中完全不溶，而分子量73 kDa及以下的LMM片段在低离子强度缓冲液中完全可溶。LMM的蛋白水解消化模式显示在距离LMM分子末端13和30 kDa处还有另外两个蛋白酶敏感位点。这表明LMM分子内存在柔性区域，这可能是主动脉肌球蛋白折叠形式的原因所在。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/b209/1136292/d6da25fbba8c/biochemj00050-0185-b.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/b209/1136292/e03d9eceecf5/biochemj00050-0181-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/b209/1136292/bfbf0ea6e875/biochemj00050-0182-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/b209/1136292/9273859477fb/biochemj00050-0182-b.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/b209/1136292/a445e809f271/biochemj00050-0183-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/b209/1136292/51a3764bb7fc/biochemj00050-0184-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/b209/1136292/b0e8492236dd/biochemj00050-0184-b.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/b209/1136292/0baf08bda60b/biochemj00050-0185-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/b209/1136292/d6da25fbba8c/biochemj00050-0185-b.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/b209/1136292/e03d9eceecf5/biochemj00050-0181-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/b209/1136292/bfbf0ea6e875/biochemj00050-0182-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/b209/1136292/9273859477fb/biochemj00050-0182-b.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/b209/1136292/a445e809f271/biochemj00050-0183-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/b209/1136292/51a3764bb7fc/biochemj00050-0184-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/b209/1136292/b0e8492236dd/biochemj00050-0184-b.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/b209/1136292/0baf08bda60b/biochemj00050-0185-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/b209/1136292/d6da25fbba8c/biochemj00050-0185-b.jpg

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Unfolding domains in smooth muscle myosin rod.
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