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从蓝藻鱼腥藻中纯化铁超氧化物歧化酶，并通过免疫金标记定位酶在异形胞中的位置。

Purification of iron superoxide dismutase from the cyanobacterium Anabaena cylindrica Lemm. and localization of the enzyme in heterocysts by immunogold labeling.

机构信息

Dipartimento di Biologia, II Università di Roma 'Tor Vergata', Via E. Carnevale, I-00173, Roma, Italy.

出版信息

Planta. 1992 Jul;187(4):438-44. doi: 10.1007/BF00199961.

DOI:10.1007/BF00199961
PMID:24178137
Abstract

Iron superoxide dismutase (Fe-SOD; EC 1.15.1.1) was isolated from the nitrogen-fixing cyanobacterium Anabaena cylindrica Lemm. Polyacrylamide gel electrophoresis separated the purified protein into three closely running, enzymatically active bands. The molecular weight of the enzyme was estimated by gel filtration to be about 40 kDa. Polyclonal antibodies were produced by immunization of rabbits with the isolated enzyme, and were purified on a column of protein A-Sepharose. The Fe-SOD antibody reacted with the purified Fe-SOD and also specifically recognized the protein in extracts of A. cylindrica. In the extracts, anti-Fe-SOD did not cross-react with Mn-SOD, an enzyme which belongs to an SOD class displaying high homology of primary and three-dimensional structure with respect to Fe-SOD. Iron superoxide dismutase was localized in heterocysts by immunogold labeling and transmission electron microscopy. These results are the first in-situ evidence for the presence of SOD in the cells specialized for nitrogenase activity.

摘要

从固氮蓝藻鱼腥藻中分离出铁超氧化物歧化酶（Fe-SOD；EC 1.15.1.1）。聚丙烯酰胺凝胶电泳将纯化的蛋白质分离成三个紧密运行的、具有酶活性的条带。通过凝胶过滤法估计该酶的分子量约为 40 kDa。用分离的酶对兔子进行免疫产生多克隆抗体，并在蛋白 A-琼脂糖柱上进行纯化。Fe-SOD 抗体与纯化的 Fe-SOD 反应，并且特异性识别鱼腥藻提取物中的蛋白质。在提取物中，抗 Fe-SOD 与 Mn-SOD 不发生交叉反应，Mn-SOD 是一种 SOD 酶，其一级和三维结构与 Fe-SOD 具有高度同源性。通过免疫金标记和透射电子显微镜将铁超氧化物歧化酶定位于异形胞中。这些结果是首例关于专门用于固氮酶活性的细胞中存在 SOD 的原位证据。

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