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首页> 外文期刊>Protoplasma: An International Journal of Cell Biology >Superoxide dismutase, peroxidase, and germin-like protein activity in plasma membranes and apoplast of maize roots
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Superoxide dismutase, peroxidase, and germin-like protein activity in plasma membranes and apoplast of maize roots

机译：玉米根质膜和质外体中的超氧化物歧化酶，过氧化物酶和胚芽蛋白样蛋白活性

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摘要

The analysis of plasma membranes from maize roots by native gel electrophoresis revealed the existence of Mn-containing 120 kDa and CuZn-containing 70, 40, and 15 kDa superoxide dismutase (SOD) isoform activities. Isoelectric focusing of the plasma membranes differentiated anionic SOD isoforms with a pI of about 5 and cationic SOD isoforms at pI 8.6. Solubilization of the plasma membrane proteins further separated the cationic SOD into pI 8.6, 8.2, 8.4, and 7.2 isoforms. Double staining for both SOD and peroxidase activities showed an overlap of these activities only in the case of the high-molecular-mass (ca. 120 kDa) isoforms. High-temperature treatments demonstrated that the 120 kDa isoform was active even at 100 degrees C, indicating that it was a germin-like protein with superoxide-dismutating activity, different from the peroxidase with a similar molecular mass and the lower-molecular-mass CuZn-containing superoxide dismutases. These results are compared to those obtained from whole-tissue extract and apoplastic fluid.
机译：通过天然凝胶电泳分析玉米根的质膜，发现存在含锰的120 kDa和含铜锌的70、40和15 kDa超氧化物歧化酶（SOD）同工型活性。质膜的等电聚焦区分了pI约为5的阴离子SOD亚型和pI 8.6的阳离子SOD亚型。质膜蛋白的增溶进一步将阳离子SOD分离为pI 8.6、8.2、8.4和7.2亚型。 SOD和过氧化物酶活性的双重染色仅在高分子质量（约120 kDa）同工型的情况下才显示出这些活性的重叠。高温处理表明120 kDa的同工型甚至在100摄氏度时仍具有活性，表明它是一种具有超氧化物歧化活性的胚芽状蛋白，不同于具有相似分子量和过低分子量CuZn的过氧化物酶。含有超氧化物歧化酶。将这些结果与从全组织提取物和质外生流体中获得的结果进行比较。

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