Department of Genetics, North Carolina State University, Raleigh, North Carolina 27650.
Plant Physiol. 1983 Sep;73(1):31-5. doi: 10.1104/pp.73.1.31.
The chloroplast-associated form of superoxide dismutase from maize (Zea mays L.) (SOD-1) has been purified by a stepwise procedure consisting of (NH(4))(2)SO(4) fractionation, G-100 Sephadex gel filtration, DEAE-Sephacel chromatography, and hydroxylapatite chromatography. This procedure resulted in a single band on sodium dodecyl sulfate-polyacrylamide gels indicating that the preparation is homogeneous. The holoenzyme molecular weight was estimated at 31,000 to 33,000 by gel filtration. The subunit molecular weight of this dimeric protein was estimated at 14,500 on sodium dodecyl sulfate-polyacrylamide gels. Studies involving amino acid composition analysis, immunological cross-reactivity, in vitro subunit hybridizations, and H(2)O(2) sensitivity indicate that SOD-1 differs significantly from SOD-2 and SOD-4, the other cupro-zinc forms of SOD from maize. The possible physiological role of SOD-1 within the chloroplast is discussed.
来自玉米（Zea mays L.）的叶绿体相关形式的超氧化物歧化酶（SOD-1）已通过逐步程序进行纯化，该程序包括（NH 4 ） 2 SO 4 分级，G-100 葡聚糖凝胶过滤，DEAE-葡聚糖凝胶色谱和羟基磷灰石色谱。该程序在十二烷基硫酸钠-聚丙烯酰胺凝胶上产生一条带，表明该制剂是均匀的。通过凝胶过滤，全酶的分子量估计在 31,000 到 33,000 之间。该二聚体蛋白的亚基分子量在十二烷基硫酸钠-聚丙烯酰胺凝胶上估计为 14,500。涉及氨基酸组成分析，免疫交叉反应，体外亚基杂交和 H 2 O 2 敏感性的研究表明，SOD-1 与 SOD-2 和 SOD-4（玉米的其他铜锌形式的 SOD）有很大的不同。讨论了 SOD-1 在叶绿体中的可能生理作用。
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