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关于蓝藻鱼腥藻核酮糖-1,5-二磷酸羧化酶亚基结构的研究。

Studies on the subunit structure of ribulose-1,5-diphosphate carboxylase from the blue-green alga Microcystis aeruginosa.

机构信息

Department of Biological Sciences, University of Dundee, DD1 4HN, Dundee, UK.

出版信息

Planta. 1977 Jan;136(1):61-4. doi: 10.1007/BF00387926.

Abstract

Ribulose-1,5-diphosphate carboxylase (EC 4.1.1.39) has been purified from the unicellular blue-green alga Microcystis aeruginosa by ammonium sulphate precipitation, followed by linear sucrose density gradient centrifugation. The enzyme has a molecular weight of 518, 000 and contains two types of subunits (large, 50,000 and small, 14,000) as shown by sodium dodecyl sulphate polyacrylamide gel electrophoresis. The enzyme from this photosynthetic prokaryote thus appears to resemble closely the ribulose, diphosphate carboxylase of eukaryotic microalgal chloroplasts in quaternary structure.

摘要

核酮糖-1,5-二磷酸羧化酶(EC 4.1.1.39)已通过硫酸铵沉淀,随后进行线性蔗糖密度梯度离心,从单细胞蓝绿藻微囊藻中纯化出来。该酶的分子量为 518,000,通过十二烷基硫酸钠聚丙烯酰胺凝胶电泳显示含有两种类型的亚基(大亚基,50,000 和小亚基,14,000)。因此,这种光合原核生物的酶在四级结构上似乎与真核微藻叶绿体的核酮糖-1,5-二磷酸羧化酶非常相似。

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