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首页> 外文期刊>Open access Insect Physiology >Superoxide dismutase activities in the midgut of Helicoverpa armigera larvae: identification and biochemical properties of a manganese superoxide dismutase
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Superoxide dismutase activities in the midgut of Helicoverpa armigera larvae: identification and biochemical properties of a manganese superoxide dismutase

机译：棉铃虫幼虫中肠超氧化物歧化酶活性：锰超氧化物歧化酶的鉴定及生化特性

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Abstract: Insects possess a complex network of enzymatic antioxidant systems protecting against reactive oxygen species generated during stress. Superoxide dismutases (SODs) are vital antioxidant enzymes converting superoxide into oxygen and hydrogen peroxide. Helicoverpa armigera is a polyphagous insect and has developed resistance to various phytochemicals and pesticides. Although SODs are studied in several insect species, their characterization has been reported in only a few insect species. Here, we attempted to identify and characterize SOD activity from H. armigera. Electrophoretic separation followed by nitroblue tetrazolium staining revealed the presence of five SOD activity isoforms in the midgut of H. armigera larvae. Total SOD activity was measured at the different larval developmental stages and found maximum at fourth instar and further declined at sixth instar. Total SOD activity was significantly increased by metal ions Mn, Fe, Zn, and Cu and reduced by Ca and Pb. The isoform with highest activity was identified as manganese SOD (MnSOD) because it was found insensitive to H2O2. The identified MnSOD was partially purified and characterized. After gel filtration chromatography, specific activity of the purified enzyme was found to be 6,348.0 U/mg/min with 26.61% yield. The molecular mass of purified enzyme was calculated to be ~29.3 kDa by sodium dodecyl sulfate polyacrylamide gel electrophoresis. The optimum pH and temperature for the SOD activity were found to be around 11 and 60°C, respectively. The study could be useful to further understand the functional significance of SODs in the antioxidant mechanism of H. armigera.
机译：摘要：昆虫拥有复杂的酶促抗氧化剂系统网络，可防御应激过程中产生的活性氧。超氧化物歧化酶（SOD）是重要的抗氧化剂酶，可将超氧化物转化为氧气和过氧化氢。棉铃虫（Helicoverpa armigera）是一种多食性昆虫，对各种植物化学物质和杀虫剂具有抗药性。尽管已在几种昆虫中研究了SOD，但仅在少数几种昆虫中报告了其特征。在这里，我们试图鉴定和表征棉铃虫的SOD活性。电泳分离，然后进行硝基蓝四唑鎓染色，揭示了棉铃虫幼虫中肠中存在5种SOD活性同工型。在不同的幼虫发育阶段对总SOD活性进行了测量，在第四龄时发现最大，而在第六龄时进一步下降。金属离子Mn，Fe，Zn和Cu显着提高了总SOD活性，而Ca和Pb降低了总SOD活性。具有最高活性的同工型被鉴定为锰超氧化物歧化酶（MnSOD），因为发现它对H2O2不敏感。鉴定出的MnSOD被部分纯化和表征。经凝胶过滤层析后，发现纯化的酶的比活为6,348.0 U / mg / min，产率为26.61％。通过十二烷基硫酸钠聚丙烯酰胺凝胶电泳计算出纯化的酶的分子量为〜29.3 kDa。发现SOD活性的最佳pH和温度分别为约11和60℃。该研究可能有助于进一步了解SOD在棉铃虫抗氧化机理中的功能意义。

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