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水稻RuBP羧化酶的提纯及电泳性质分析
PURIFICATION AND ELECTROPHORESIS ANALYSIS OF RUBPCASE FROM RICE
【摘要】 RuBP(1、5—二磷酸核酮础)羧化酶,在绿色植物的光合过程中起着重要作用。我们采用Sephadex 柱层析法从水稻中分离和纯化了该酶,并获得了结晶。经电泳鉴定为一条酶带。该酶结品又经解聚,S—羧甲基化和聚丙烯酰胺凝胶等电聚焦电泳分析呈5条带,3条为大亚基肽链,2条为小亚基肽链。
【Abstract】 RuBPCase called ribulose 1、5-bisphosphate carboxylase-oxygenase or Fraction I protein or Rubisco.lt is playing an importent role in photosynthesis of green plant.We have used Sephadex column to purify this enzyme from rice and obtained crytal.It was indicated to be pure in polyacrylamide gel electrophorsis.The poly- peptide composition of S-carboxymethylated rice BuBPCase which is revealed by isoelectrofocusing is 8 M urea,appeared to have five compositions.Three bands is large subunits(LS).Two bands is small subunits(SS).
- 【文献出处】 上海农学院学报 , 编辑部邮箱 ,1988年04期
- 【被引频次】3
- 【下载频次】140