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首页> 外文期刊>Aquaculture Research >A chimeric recombinant crustacean hyperglycemic hormone from Litopenaeus schmitti (Burkenroad) obtained as C-terminus fusion protein boost hemolymph glucose concentration in Litopenaeus vannamei (Boone).
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A chimeric recombinant crustacean hyperglycemic hormone from Litopenaeus schmitti (Burkenroad) obtained as C-terminus fusion protein boost hemolymph glucose concentration in Litopenaeus vannamei (Boone).

机译：来自C. Litopenaeus schmitti（Burkenroad）的嵌合重组甲壳类高血糖激素，作为C端融合蛋白获得，可提高凡纳滨对虾（Boone）的血淋巴葡萄糖浓度。

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摘要

To date, no hormonal treatments are available for control of shrimp reproduction and only eyestalk ablation is of practical use. The crustacean hyperglycemic hormone (CHH) is the most abundant neuropeptide of the eyestalk CHH family. It plays an important role in the regulation of hemolymph glucose levels, as its principal function, but it is also implicated in additional physiological processes such as moulting and reproduction. In the present study, the cDNA encoding Litopenaeus schmitti (Burkenroad) mature CHH was cloned into the Escherichia coli pTYB2 expression vector. Using this strategy we have obtained, for the first time, the recombinant CHH from L. schmitti with its C-terminus fused to an intein tag. The expected fused protein of about 63 KDa was expressed in E. coli forming inclusion bodies. It was purified in a soluble form by electroelution following molecular size fractionation in sodium dodecil sulphate polyacrylamide gel electrophoresis. The ability of the chimeric CHH protein to elevate glucose levels in the hemolymph of the eyestalk-ablated Litopenaeus vannamei (Boone) shrimps indicates that its biological activity as hyperglycemic protein is preserved. The results provide an alternative tool to obtain soluble recombinant proteins from the CHH family of neuropeptides to get a better understanding of shrimp endocrinology.
机译：迄今为止，尚无激素治疗可用于控制虾的繁殖，只有眼柄消融才是实际应用。甲壳类高血糖激素（CHH）是眼球CHH家族中最丰富的神经肽。作为其主要功能，它在调节血淋巴葡萄糖水平中起着重要作用，但也与蜕皮和繁殖等其他生理过程有关。在本研究中，将编码施托对虾（Burkenroad）成熟CHH的cDNA克隆到大肠杆菌pTYB2表达载体中。使用这种策略，我们首次获得了来自施密特氏菌的重组CHH，其C末端融合了intein标签。预期的约63KDa的融合蛋白在大肠杆菌中表达，形成包涵体。在十二烷基硫酸钠硫酸钠聚丙烯酰胺凝胶电泳中通过分子大小分级分离后，通过电洗脱将其纯化为可溶形式。嵌合的CHH蛋白提高眼柄切除的凡纳滨对虾（Boone）虾的血淋巴中葡萄糖水平的能力表明，它保留了作为高血糖蛋白的生物学活性。结果为从CHH家族神经肽中获得可溶性重组蛋白提供了另一种工具，以更好地了解虾的内分泌。

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