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小麦叶绿体中CTK结合蛋白的纯化

ISOLATION AND PURIFICATION OF CYTOKININ-BINDING PROTEIN FROM WHEAT CHLOROPLASTS
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摘要 小麦叶绿体膜蛋白经NaCl解离后,0-30%饱和度的硫酸铵沉淀组分过BA-sepharose6B柱,6BA溶液专一冼脱结合部分,结合蛋白经聚丙烯酰胺凝胶电泳,银染色呈单带,分子量约为250kD,SDS-聚丙烯酰胺凝胶电泳呈现两条带,分子量分别为66kD和60kD。结果表明,小麦叶绿体中的CTK结合蛋白可能是由两种不同亚基组成的。 The extract of wheat chloroplast membrane proteins was precipitated by different saturation of (NH_4)_2SO_4. Pellet of 0-30% saturation showing high binding activity to ^(?)H-6BA was loaded on the affinity chromatography column which was prepared by coupling 6BA to epoxy activated sepharose 6B. The CTK-binding protein was eluted from the BA-sepharose 6B column with Tris buffer containing 0.1 mmol/L 6BA. It showed a single protein band on PAGE and the apparent molecular weight was about 250kD. Two bands with molecular weight of 60kD and 66kD were detected on SDS-PAGE. It was supposed that the protomer of CTK-binding protein was a tetramer of two subunits.
出处 《Acta Botanica Sinica》 CSCD 1991年第10期744-749,共6页 Acta Botanica Sinica(植物学报:英文版)
基金 国家自然科学基金资助项目
关键词 小麦 叶绿体 CTK结合蛋白 提纯 Wheat chloroplast Cytokinin-binding protein Affinity chromatography
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参考文献4

  • 1黄海,实验生物学报,1988年,21卷,155页
  • 2黄海,植物生理学报,1984年,10卷,347页
  • 3张龙翔,生化实验方法和技术,1981年
  • 4Chen C M,Euv J Biochem,1980年,108卷,379页

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