Molecular weight of Nephila clavata spider silk

Molecular weight of Nephila clavata spider silk
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Nephila clavata 蜘蛛丝的分子量

DOI:
10.1038/pj.2015.10
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发表时间:
2015
期刊:
影响因子:
2.8
通讯作者:
Takashi Matsuhira and Shigeyoshi Osaki
Takashi Matsuhira and Shigeyoshi Osaki
中科院分区:
化学3区
文献类型:
--
作者:
Shigeyoshi Osaki;Keizo Yamamoto;Takashi Matsuhira and Hiromi Sakai;大崎茂芳;大崎茂芳;大崎茂芳;Takashi Matsuhira and Shigeyoshi Osaki

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经测定棒形络新妇蜘蛛丝的分子量约为1000。600 kDa,在非还原条件下,对应于其天然状态,使用十二烷基硫酸钠聚丙烯酰胺凝胶电泳法和最大分子量为500 kDa的蛋白质标记物。向蜘蛛丝溶液中加入2-巯基乙醇,可使蜘蛛丝的分子量从约1000降低到约1000。600 kD左右。270 kDa。分子量的这种急剧下降归因于作为还原剂的2-巯基乙醇的存在。这一发现表明,还原过程可能切断了蜘蛛丝蛋白之间形成的二硫键,然后使分子量从约100。600人左右。270 kDa。这些结果表明,N.棒形蜘蛛丝蛋白可能由两种分子量约为100的蛋白质组成。270 kDa,通过二硫键交联,并作为ca. 600 kDa。
The molecular weight of Nephila clavata spider silk was determined to be ca. 600 kDa, under unreduced conditions, corresponding to its natural state, using the sodium dodecyl sulfate polyacrylamide gel electrophoresis method and a protein marker with a maximum molecular weight of 500 kDa. The addition of 2-mercaptoethanol into the spider silk solution decreased the molecular weight from ca. 600 kDa to ca. 270 kDa. Such a dramatic decrease in the molecular weight was ascribed to the presence of 2-mercaptoethanol as a reductant. This finding indicates the possibility that the reduction process cleaved the disulfide bonds formed between the spider silk proteins and then drastically decreased the molecular weight from ca. 600 to ca. 270 kDa. These results suggest that N. clavata spider silk proteins might consist of two proteins with a molecular weight of ca. 270 kDa that are crosslinked by disulfide bonds and exist as a dimer of ca. 600 kDa.
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发表时间: 2012-04
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